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Conserved domains on  [gi|982972215|ref|XP_015316815|]
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tyrosine 3-monooxygenase isoform X1 [Bos taurus]

Protein Classification

sigma-54-dependent Fis family transcriptional regulator( domain architecture ID 10289117)

sigma-54-dependent Fis family transcriptional regulator similar to TyrR which regulates genes involved in the uptake and biosynthesis of aromatic amino acids; contains N-terminal ACT domain and C-terminal HTH domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Biopterin_H pfam00351
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
130-459 0e+00

Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.


:

Pssm-ID: 459776  Cd Length: 331  Bit Score: 709.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  130 WFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYP 209
Cdd:pfam00351   2 WFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLYP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  210 THACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 289
Cdd:pfam00351  82 THACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  290 EPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLS 369
Cdd:pfam00351 162 EPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYALS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  370 EEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPHAIRRALDGVQD 449
Cdd:pfam00351 242 DKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIKG 321
                         330
                  ....*....|
gi 982972215  450 EMQALAHALN 459
Cdd:pfam00351 322 DLDILTDALE 331
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
9-121 9.40e-28

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


The actual alignment was detected with superfamily member cd04930:

Pssm-ID: 471857 [Multi-domain]  Cd Length: 115  Bit Score: 106.71  E-value: 9.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215   9 RQSLIQDARKEREKAEAAASSSESAEAGSLVERDGKAV---LTLLFALRpTKPPALTRAIKVFETFEAHLHHLETRPAqp 85
Cdd:cd04930    1 KQSLIEDARKEREDASLTEDAEDDLDSEVFEEKEGKAVpqkATLLFSLK-EGFSSLSRILKVFETFEAKIHHLESRPS-- 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 982972215  86 lRAGSPPLECFVRCEVPGPVVPALLSALRRVAEDVR 121
Cdd:cd04930   78 -RKEGGDLEVLVRCEVHRSDLLQLISSLRQVAEDVR 112
 
Name Accession Description Interval E-value
Biopterin_H pfam00351
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
130-459 0e+00

Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.


Pssm-ID: 459776  Cd Length: 331  Bit Score: 709.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  130 WFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYP 209
Cdd:pfam00351   2 WFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLYP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  210 THACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 289
Cdd:pfam00351  82 THACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  290 EPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLS 369
Cdd:pfam00351 162 EPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYALS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  370 EEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPHAIRRALDGVQD 449
Cdd:pfam00351 242 DKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIKG 321
                         330
                  ....*....|
gi 982972215  450 EMQALAHALN 459
Cdd:pfam00351 322 DLDILTDALE 331
Tyr_3_monoox TIGR01269
tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member ...
9-459 0e+00

tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tryptophan 5-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria.


Pssm-ID: 130336 [Multi-domain]  Cd Length: 457  Bit Score: 656.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215    9 RQSLIQDARKEREKAEAAASSSESAEAgSLVERDGKAVLTLLFALRPTKPPALTRAIKVFETFEAHLHHLETRPAQPLRA 88
Cdd:TIGR01269   1 KQSTVELARNEKDYGRIHSIIINFHPI-THEQDSEAAMQNNQFYIRTKEISSLHRILKYIETFKLNLVHFETRPTRTLSN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215   89 GSPPLECFVRCEVPGPVVPALLSALRR----VAEDVRAAGESKVLWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAY 164
Cdd:TIGR01269  80 ADVDYSCLITLEANEINMSLLIESLRGnsfiSGINLLNNQNVKEDWFPKHISELDKCQHLLTKFQPDLDTDHPGFHDKVY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  165 RQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLERFCGYREDRIPQLEDVSRFL 244
Cdd:TIGR01269 160 RQRREAIAEIAFQYKYGDPIPEVEYTKEEIETWRLVFTTMKDLHASHACREYIDAFQLLEKYCNYNSESIPQLQTISEFL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  245 KERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVS 324
Cdd:TIGR01269 240 HRTTGFRLRPVAGLLSARDFLASLAFRVFQCTQYIRHHSSPMHTPEPDCIHELLGHMPMLADRQFAQFSQEIGLASLGAS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  325 DEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLSEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSD 404
Cdd:TIGR01269 320 EEEIEKLSTLYWFTVEFGLCKENGETKAYGAGLLSSYGELEHAFSDLSEKRPFNPNDAAVQPYQDQGYQKIYFVTESFED 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 982972215  405 AKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPHAIRRALDGVQDEMQALAHALN 459
Cdd:TIGR01269 400 AKRKLRNYINTSGRPFIVRFDPITETVEVLDRFSKRKELLKHVKEEIGQLTTALN 454
eu_TyrOH cd03345
Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino ...
130-427 0e+00

Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tryptophan hydroxylase (TrpOH). TyrOH catalyzes the conversion of tyrosine to L-dihydroxyphenylalanine (L-DOPA), the rate-limiting step in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline.


Pssm-ID: 239461  Cd Length: 298  Bit Score: 646.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 130 WFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYP 209
Cdd:cd03345    1 WFPRHISELDKCHHLVTKYEPDLDLDHPGFSDKVYRERRKLIAEIAFQYKHGDPIPRVEYTAEEIATWKEVYKTLKDLHA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 210 THACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 289
Cdd:cd03345   81 THACKEYLDAFQLLEKECGYSEDRIPQLEDVSEFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 290 EPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLS 369
Cdd:cd03345  161 EPDCCHELLGHVPMLADPTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKENGELKAYGAGLLSSYGELLHALS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 982972215 370 EEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY 427
Cdd:cd03345  241 DEPEHRPFDPAATAVQPYQDQTYQPIYFVSESFSDAKDKLRNYASTMKRPFSVRYDPY 298
PhhA COG3186
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];
179-404 7.41e-84

Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];


Pssm-ID: 442419  Cd Length: 279  Bit Score: 259.36  E-value: 7.41e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 179 KQGDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLerfcGYREDRIPQLEDVSRFLKERTGFQLRPVAGL 258
Cdd:COG3186   16 RYTDPQGYIDYTAEEHAVWRRLYRRQVALLPGRACDEYLDGLEKL----GLPADRIPQLDEVNERLKALTGWRVVAVPGL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 259 LSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVS--DEEIEKLSTLYW 336
Cdd:COG3186   92 IPPDAFFELLANRRFPVATFIRTPEEIDYLPEPDIFHEVFGHVPLLTNPVFADFLQAYGEAGLKASklDSELALLARLYW 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982972215 337 FTVEFGLCKQNGEVKAYGAGLLSSYGELLHSL-SEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSD 404
Cdd:COG3186  172 FTVEFGLIGTPEGLRIYGAGILSSPGESEYALeSDEPNRIPFDLERVMRTPYRIDIYQPTYFVIDSFDQ 240
phhA PRK11913
phenylalanine 4-monooxygenase; Reviewed
161-404 1.67e-83

phenylalanine 4-monooxygenase; Reviewed


Pssm-ID: 237020  Cd Length: 275  Bit Score: 258.26  E-value: 1.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 161 DQAYRQRRKLIAEIAFQYKQGDPIphVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLerfcGYREDRIPQLEDV 240
Cdd:PRK11913   1 DAAYRARRDAGMEKAADYTADQPW--IDYTAEEHAIWQTLYERQLALLPGRACDEFLEGLEAL----GLPKDRIPQLDEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 241 SRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLAS 320
Cdd:PRK11913  75 NRVLQAATGWQVVPVPGLIPFDVFFELLANRRFPVATFIRRPEELDYLQEPDIFHDVFGHVPLLTNPVFADFMQAYGKLG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 321 LGVSDEE-IEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSL-SEEPEIRAFDPDAAAVQPYQDQTYQPVYFV 398
Cdd:PRK11913 155 LRASKEGrLEFLARLYWFTVEFGLIRTPGGLRIYGAGILSSPGETLYALeSDSPNRRPFDLERVMRTPYRIDIFQPTYFV 234

                 ....*.
gi 982972215 399 SESFSD 404
Cdd:PRK11913 235 IDSFEQ 240
ACT_TH cd04930
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine ...
9-121 9.40e-28

ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH); ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH). TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines (dopamine, noradrenaline and adrenaline), functioning as hormones and neurotransmitters. The enzyme is not regulated by its amino acid substrate, but instead by phosphorylation at several serine residues located N-terminal of the ACT domain, and by feedback inhibition by catecholamines at the active site. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153202 [Multi-domain]  Cd Length: 115  Bit Score: 106.71  E-value: 9.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215   9 RQSLIQDARKEREKAEAAASSSESAEAGSLVERDGKAV---LTLLFALRpTKPPALTRAIKVFETFEAHLHHLETRPAqp 85
Cdd:cd04930    1 KQSLIEDARKEREDASLTEDAEDDLDSEVFEEKEGKAVpqkATLLFSLK-EGFSSLSRILKVFETFEAKIHHLESRPS-- 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 982972215  86 lRAGSPPLECFVRCEVPGPVVPALLSALRRVAEDVR 121
Cdd:cd04930   78 -RKEGGDLEVLVRCEVHRSDLLQLISSLRQVAEDVR 112
 
Name Accession Description Interval E-value
Biopterin_H pfam00351
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
130-459 0e+00

Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.


Pssm-ID: 459776  Cd Length: 331  Bit Score: 709.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  130 WFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYP 209
Cdd:pfam00351   2 WFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLYP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  210 THACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 289
Cdd:pfam00351  82 THACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYTP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  290 EPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLS 369
Cdd:pfam00351 162 EPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYALS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  370 EEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPHAIRRALDGVQD 449
Cdd:pfam00351 242 DKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIKG 321
                         330
                  ....*....|
gi 982972215  450 EMQALAHALN 459
Cdd:pfam00351 322 DLDILTDALE 331
Tyr_3_monoox TIGR01269
tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member ...
9-459 0e+00

tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tryptophan 5-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria.


Pssm-ID: 130336 [Multi-domain]  Cd Length: 457  Bit Score: 656.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215    9 RQSLIQDARKEREKAEAAASSSESAEAgSLVERDGKAVLTLLFALRPTKPPALTRAIKVFETFEAHLHHLETRPAQPLRA 88
Cdd:TIGR01269   1 KQSTVELARNEKDYGRIHSIIINFHPI-THEQDSEAAMQNNQFYIRTKEISSLHRILKYIETFKLNLVHFETRPTRTLSN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215   89 GSPPLECFVRCEVPGPVVPALLSALRR----VAEDVRAAGESKVLWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAY 164
Cdd:TIGR01269  80 ADVDYSCLITLEANEINMSLLIESLRGnsfiSGINLLNNQNVKEDWFPKHISELDKCQHLLTKFQPDLDTDHPGFHDKVY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  165 RQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLERFCGYREDRIPQLEDVSRFL 244
Cdd:TIGR01269 160 RQRREAIAEIAFQYKYGDPIPEVEYTKEEIETWRLVFTTMKDLHASHACREYIDAFQLLEKYCNYNSESIPQLQTISEFL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  245 KERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVS 324
Cdd:TIGR01269 240 HRTTGFRLRPVAGLLSARDFLASLAFRVFQCTQYIRHHSSPMHTPEPDCIHELLGHMPMLADRQFAQFSQEIGLASLGAS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  325 DEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLSEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSD 404
Cdd:TIGR01269 320 EEEIEKLSTLYWFTVEFGLCKENGETKAYGAGLLSSYGELEHAFSDLSEKRPFNPNDAAVQPYQDQGYQKIYFVTESFED 399
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 982972215  405 AKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPHAIRRALDGVQDEMQALAHALN 459
Cdd:TIGR01269 400 AKRKLRNYINTSGRPFIVRFDPITETVEVLDRFSKRKELLKHVKEEIGQLTTALN 454
eu_TyrOH cd03345
Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino ...
130-427 0e+00

Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tryptophan hydroxylase (TrpOH). TyrOH catalyzes the conversion of tyrosine to L-dihydroxyphenylalanine (L-DOPA), the rate-limiting step in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline.


Pssm-ID: 239461  Cd Length: 298  Bit Score: 646.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 130 WFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYP 209
Cdd:cd03345    1 WFPRHISELDKCHHLVTKYEPDLDLDHPGFSDKVYRERRKLIAEIAFQYKHGDPIPRVEYTAEEIATWKEVYKTLKDLHA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 210 THACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 289
Cdd:cd03345   81 THACKEYLDAFQLLEKECGYSEDRIPQLEDVSEFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 290 EPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLS 369
Cdd:cd03345  161 EPDCCHELLGHVPMLADPTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKENGELKAYGAGLLSSYGELLHALS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 982972215 370 EEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPY 427
Cdd:cd03345  241 DEPEHRPFDPAATAVQPYQDQTYQPIYFVSESFSDAKDKLRNYASTMKRPFSVRYDPY 298
Phe4hydrox_tetr TIGR01268
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ...
45-461 0e+00

phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form of phenylalanine-4-hydroxylase, as found in metazoans. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. It is closely related to metazoan tyrosine 3-monooxygenase and tryptophan 5-monoxygenase, and more distantly to monomeric phenylalanine-4-hydroxylases of some Gram-negative bacteria. The member of this family from Drosophila has been described as having both phenylalanine-4-hydroxylase and tryptophan 5-monoxygenase activity (. However, a Drosophila member of the tryptophan 5-monoxygenase clade has subsequently been discovered.


Pssm-ID: 130335 [Multi-domain]  Cd Length: 436  Bit Score: 515.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215   45 AVLTLLFALRpTKPPALTRAIKVFETFEAHLHHLETRPAQPLRAGsppLECFVRCEVPGPvvPALLSALRRVAEDVRAA- 123
Cdd:TIGR01268  15 AKTSLIFSLK-EEAGALAETLKLFQAHDVNLTHIESRPSKTHPGE---YEFFVEFDEASD--RKLEGVIEHLRQKAEVTv 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  124 ---------GESKVLWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEET 194
Cdd:TIGR01268  89 nilsrdnkqNKDSVPWFPRKINDIDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAFNYKHGQPIPRVEYTDEEI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  195 ATWKEVYSTLRGLYPTHACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQ 274
Cdd:TIGR01268 169 ATWRTVFNNLTVLYPTHACQEYNHIFPLLQQNCGFREDNIPQLEDVSQFLQDCTGFTLRPVAGLLSSRDFLAGLAFRVFH 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  275 CTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYG 354
Cdd:TIGR01268 249 STQYIRHHSKPMYTPEPDICHELLGHVPLFADVEFAQFSQEIGLASLGAPDDYIEKLATLYWFTIEFGLCKQDGEKKAYG 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  355 AGLLSSYGELLHSLSEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVL 434
Cdd:TIGR01268 329 AGLLSSFGELQYCLSDKPEVVDFDPEVTCVTKYPITEFQPLYFLAESFEDAKEKLKSFAATIPRPFSVRYNAYTQRVEIL 408
                         410       420
                  ....*....|....*....|....*..
gi 982972215  435 DSPHAIRRALDGVQDEMQALAHALNAI 461
Cdd:TIGR01268 409 DKKAQLQRLADDIRSEISILQEALGKL 435
eu_PheOH cd03347
Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent ...
130-434 4.89e-176

Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic phenylalanine-4-hydroxylase (pro_PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH catalyzes the first and rate-limiting step in the metabolism of the amino acid L-phenylalanine (L-Phe), the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor. The catalytic activity of the tetrameric enzyme is tightly regulated by the binding of L-Phe and BH4 as well as by phosphorylation. Mutations in the human enzyme are linked to a severe variant of phenylketonuria.


Pssm-ID: 239463  Cd Length: 306  Bit Score: 495.04  E-value: 4.89e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 130 WFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYP 209
Cdd:cd03347    2 WFPRTIQDLDRFANQILSYGAELDADHPGFKDPVYRARRKEFADIAYNYKHGQPIPRVEYTEEEKKTWGTVFRELKSLYP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 210 THACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 289
Cdd:cd03347   82 THACYEYNHVFPLLEKNCGFSEDNIPQLEDVSNFLQTCTGFRLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHPSKPMYTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 290 EPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLS 369
Cdd:cd03347  162 EPDICHELLGHVPLFADPSFAQFSQEIGLASLGAPDEYIEKLATVYWFTVEFGLCKQGGSIKAYGAGLLSSFGELQYCLS 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982972215 370 EEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVL 434
Cdd:cd03347  242 DKPELLPFEPEKTAVTKYPITEFQPLYYVAESFEDAKEKLRNFAATIPRPFSVRYNPYTQRIEVL 306
Trp_5_monoox TIGR01270
tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a ...
40-462 2.36e-173

tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tyrosine 3-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130337 [Multi-domain]  Cd Length: 464  Bit Score: 494.37  E-value: 2.36e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215   40 ERDGKAVLTLLFALRpTKPPALTRAIKVFETFEAHLHHLETRPAQplRAGSPPLECFVRCEVPGPVVPALLSALRR---- 115
Cdd:TIGR01270  25 EEEGVQRLSIIFSLS-NVVGDLSKAIAIFQDRHINILHLESRDSK--DGTSKTMDVLVDVELFHYGLQEAMDLLKSgldv 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  116 ---------------VAEDVRAAGESKVLWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQ 180
Cdd:TIGR01270 102 hevsspirptlieaqYTEPGSDDATTGVPWFPKKISDLDKCANRVLMYGSELDADHPGFKDTEYRKRRMMFADLALNYKH 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  181 GDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLS 260
Cdd:TIGR01270 182 GEPIPRVEYTEEERKTWGTIYRELRRLYKTHACKEFLDNLPLLEKYCGYREDNIPQLEDVSKFLKAKTGFRLRPVAGYLS 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  261 ARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVE 340
Cdd:TIGR01270 262 ARDFLSGLAFRVFHCTQYVRHSADPFYTPEPDTCHELLGHMPLLADPSFAQFSQEIGLASLGASEEDIKKLATLYFFTIE 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  341 FGLCKQ-NGEVKAYGAGLLSSYGELLHSLSEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASRIQRP 419
Cdd:TIGR01270 342 FGLCKQdDEQFKVYGAGLLSSVAELQHALSGSAKIKPFDPDRVCEQECLITTFQNAYFYTRSFEEAKEKMREFTNTIKRP 421
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 982972215  420 FSVKFDPYTLAIDVLDSPHAIRRALDGVQDEMQALAHALNAIS 462
Cdd:TIGR01270 422 FGVRYNPYTESVEVLKNSKSITLAVNELRSDLNLVAGALHKIS 464
eu_TrpOH cd03346
Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino ...
130-413 4.82e-161

Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tyrosine hydroxylase (TyrOH). TrpOH oxidizes L-tryptophan to 5-hydroxy-L-tryptophan, the rate-limiting step in the biosynthesis of serotonin (5-hydroxytryptamine), a widely distributed hormone and neurotransmitter.


Pssm-ID: 239462  Cd Length: 287  Bit Score: 456.57  E-value: 4.82e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 130 WFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQAYRQRRKLIAEIAFQYKQGDPIPHVEYTAEETATWKEVYSTLRGLYP 209
Cdd:cd03346    2 WFPKKISDLDKCANRVLMYGSELDADHPGFKDNVYRKRRKYFADVAMNYKHGDPIPRVEYTEEEIKTWGTVYRELNRLYP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 210 THACREHLEAFELLERFCGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 289
Cdd:cd03346   82 THACREYLKNLPLLEKHCGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCTQYVRHSSDPFYTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 290 EPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSLS 369
Cdd:cd03346  162 EPDTCHELLGHVPLLADPSFAQFSQEIGLASLGASDEDIQKLATCYFFTVEFGLCKQDGQLKVYGAGLLSSIGELKHALS 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 982972215 370 EEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYA 413
Cdd:cd03346  242 GEAKVKPFDPKVTCKQECLITTFQEAYFVSESFEEAKEKMREFA 285
arom_aa_hydroxylase cd00361
Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent ...
185-408 1.35e-136

Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent enzymes that includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH), eukaryotic tyrosine hydroxylase (TyrOH) and eukaryotic tryptophan hydroxylase (TrpOH). PheOH converts L-phenylalanine to L-tyrosine, an important step in phenylalanine catabolism and neurotransmitter biosynthesis, and is linked to a severe variant of phenylketonuria in humans. TyrOH and TrpOH are involved in the biosynthesis of catecholamine and serotonin, respectively. The eukaryotic enzymes are all homotetramers.


Pssm-ID: 238215  Cd Length: 221  Bit Score: 391.53  E-value: 1.35e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 185 PHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLerfcGYREDRIPQLEDVSRFLKERTGFQLRPVAGLLSARDF 264
Cdd:cd00361    1 PRVDYTEEEHATWRTLYRRLKKLLPTHACREYLEGLELL----GLPEDRIPQLEDVSEFLKALTGWTLVPVAGLISPRDF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 265 LASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSD-EEIEKLSTLYWFTVEFGL 343
Cdd:cd00361   77 FALLAFRVFPVTQYIRHPEEPDYTPEPDIFHELFGHVPLLADPSFADFSQEYGLASLGASDlEEIEKLARLYWFTVEFGL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982972215 344 CKQNGEVKAYGAGLLSSYGELLHSLSEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKDK 408
Cdd:cd00361  157 IKEDGELKAYGAGLLSSYGELQHALSDKPKRIPFDPERVARTPYDITSFQPTYFVIESFEQLKEK 221
PhhA COG3186
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];
179-404 7.41e-84

Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];


Pssm-ID: 442419  Cd Length: 279  Bit Score: 259.36  E-value: 7.41e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 179 KQGDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLerfcGYREDRIPQLEDVSRFLKERTGFQLRPVAGL 258
Cdd:COG3186   16 RYTDPQGYIDYTAEEHAVWRRLYRRQVALLPGRACDEYLDGLEKL----GLPADRIPQLDEVNERLKALTGWRVVAVPGL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 259 LSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVS--DEEIEKLSTLYW 336
Cdd:COG3186   92 IPPDAFFELLANRRFPVATFIRTPEEIDYLPEPDIFHEVFGHVPLLTNPVFADFLQAYGEAGLKASklDSELALLARLYW 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 982972215 337 FTVEFGLCKQNGEVKAYGAGLLSSYGELLHSL-SEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSD 404
Cdd:COG3186  172 FTVEFGLIGTPEGLRIYGAGILSSPGESEYALeSDEPNRIPFDLERVMRTPYRIDIYQPTYFVIDSFDQ 240
phhA PRK11913
phenylalanine 4-monooxygenase; Reviewed
161-404 1.67e-83

phenylalanine 4-monooxygenase; Reviewed


Pssm-ID: 237020  Cd Length: 275  Bit Score: 258.26  E-value: 1.67e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 161 DQAYRQRRKLIAEIAFQYKQGDPIphVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLerfcGYREDRIPQLEDV 240
Cdd:PRK11913   1 DAAYRARRDAGMEKAADYTADQPW--IDYTAEEHAIWQTLYERQLALLPGRACDEFLEGLEAL----GLPKDRIPQLDEI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 241 SRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLAS 320
Cdd:PRK11913  75 NRVLQAATGWQVVPVPGLIPFDVFFELLANRRFPVATFIRRPEELDYLQEPDIFHDVFGHVPLLTNPVFADFMQAYGKLG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 321 LGVSDEE-IEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHSL-SEEPEIRAFDPDAAAVQPYQDQTYQPVYFV 398
Cdd:PRK11913 155 LRASKEGrLEFLARLYWFTVEFGLIRTPGGLRIYGAGILSSPGETLYALeSDSPNRRPFDLERVMRTPYRIDIFQPTYFV 234

                 ....*.
gi 982972215 399 SESFSD 404
Cdd:PRK11913 235 IDSFEQ 240
pro_PheOH cd03348
Prokaryotic phenylalanine-4-hydroxylase (pro_PheOH); a member of the biopterin-dependent ...
179-404 1.04e-64

Prokaryotic phenylalanine-4-hydroxylase (pro_PheOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes the eukaryotic proteins, phenylalanine-4-hydroxylase (eu_PheOH), tyrosine hydroxylase (TyrOH) and tryptophan hydroxylase (TrpOH). PheOH catalyzes the hydroxylation of L-Phe to L-tyrosine (L-Tyr). It uses (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) as the physiological electron donor.


Pssm-ID: 239464  Cd Length: 228  Bit Score: 208.28  E-value: 1.04e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 179 KQGDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLERFcgyrEDRIPQLEDVSRFLKERTGFQLRPVAGL 258
Cdd:cd03348    1 DVPDEQGQIDYTPEEHAVWRTLYERQAKLLPGRACDAFLEGLEKLGLP----TDRIPDFADVSERLKAATGWTVVAVPGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 259 LSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASL-GVSDEEIEKLSTLYWF 337
Cdd:cd03348   77 IPDDEFFEHLANRRFPVTNFIRRPEELDYLQEPDIFHDIFGHVPMLTNPVFADFMQAYGKGGLkATGLEDRALLARLYWY 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 982972215 338 TVEFGLCKQNGEVKAYGAGLLSSYGELLHSL-SEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSD 404
Cdd:cd03348  157 TVEFGLIQEPGGLRIYGAGILSSPGETLYALeSPDPNRIPFDLERVMRTPYRIDSFQPTYFVIDSFEQ 224
Phe4hydrox_mono TIGR01267
phenylalanine-4-hydroxylase, monomeric form; This model describes the smaller, monomeric form ...
179-407 9.11e-46

phenylalanine-4-hydroxylase, monomeric form; This model describes the smaller, monomeric form of phenylalanine-4-hydroxylase, as found in a small number of Gram-negative bacteria. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. This family is of biopterin and metal-dependent hydroxylases is related to a family of longer, multimeric aromatic amino acid hydroxylases that have additional N-terminal regulatory sequences. These include tyrosine 3-monooxygenase, phenylalanine-4-hydroxylase, and tryptophan 5-monoxygenase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130334  Cd Length: 248  Bit Score: 159.27  E-value: 9.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  179 KQGDPIPHVEYTAEETATWKEVYSTLRGLYPTHACREHLEAFELLerfcGYREDRIPQLEDVSRFLKERTGFQLRPVAGL 258
Cdd:TIGR01267   1 DFTDDQGFDHYSEEEHAVWNTLITRQLKLIEGRACQEYLDGIEQL----GLPHDRIPDFDEINRKLQATTGWRIAAVPGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215  259 LSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGVSDEE-IEKLSTLYWF 337
Cdd:TIGR01267  77 IPFQTFFEHLANRRFPVTTWLRTPEELDYLQEPDIFHDIFGHVPLLTNPVFADFTHTYGKLGLKASALGrVEMLARLYWY 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 982972215  338 TVEFGLCKQNGEVKAYGAGLLSSYGELLHSL-SEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFSDAKD 407
Cdd:TIGR01267 157 TIEFGLVETDQGKRIYGAGILSSPKETVYSLeSDEPLHVAFDLLEAMRTPYRIDIFQPLYFVLPSFKRLFD 227
ACT_TH cd04930
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine ...
9-121 9.40e-28

ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH); ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine hydroxylases (TH). TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines (dopamine, noradrenaline and adrenaline), functioning as hormones and neurotransmitters. The enzyme is not regulated by its amino acid substrate, but instead by phosphorylation at several serine residues located N-terminal of the ACT domain, and by feedback inhibition by catecholamines at the active site. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153202 [Multi-domain]  Cd Length: 115  Bit Score: 106.71  E-value: 9.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215   9 RQSLIQDARKEREKAEAAASSSESAEAGSLVERDGKAV---LTLLFALRpTKPPALTRAIKVFETFEAHLHHLETRPAqp 85
Cdd:cd04930    1 KQSLIEDARKEREDASLTEDAEDDLDSEVFEEKEGKAVpqkATLLFSLK-EGFSSLSRILKVFETFEAKIHHLESRPS-- 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 982972215  86 lRAGSPPLECFVRCEVPGPVVPALLSALRRVAEDVR 121
Cdd:cd04930   78 -RKEGGDLEVLVRCEVHRSDLLQLISSLRQVAEDVR 112
PRK14056 PRK14056
aromatic amino acid hydroxylase;
186-415 3.56e-21

aromatic amino acid hydroxylase;


Pssm-ID: 237598  Cd Length: 578  Bit Score: 96.28  E-value: 3.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 186 HVEYTAEETATWKEVystLRGLYPTHACREHLEAFELLERfCGYREDRIPQLEDVSRFLKeRTGFQLRPVAGLLSARDFL 265
Cdd:PRK14056  18 YDQYTPVDHAVWRYV---MRQNHSFLKDVAHPAYLNGLQS-TGINIERIPKVEEMNECLA-EIGWGAVAVDGFIPPVAFF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 266 ASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGL-------------------------AS 320
Cdd:PRK14056  93 EFQGHGVLPIATDIRKVENIEYTPAPDIIHEAAGHAPILADPTYAEYLRRFGEigakaisskedhdvfeavrtlsivkES 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 321 LGVSDEEIEK--------------------LSTLYWFTVEFGLCkqnGEV---KAYGAGLLSSYGELLHSLSEEPEIRAF 377
Cdd:PRK14056 173 PTSTPEEVAAaenrviekqnlvsglseaeqISRLFWWTVEYGLI---GTLdnpKIYGAGLLSSVGESKHCLTDAVEKVPF 249
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 982972215 378 DPDAAAVQPYQDQTYQPVYFVSESFSDAKDKLRSYASR 415
Cdd:PRK14056 250 SIEACTSTTYDITKMQPQLFVCPDFEELSEVLEEFAET 287
ACT_AAAH cd04904
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ...
47-121 1.07e-17

ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. PAH catalyzes the hydroxylation of L-Phe to L-Tyr, the first step in the catabolic degradation of L-Phe; TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines; and TPH catalyses the hydroxylation of L-Trp to 5-hydroxytryptophan, the rate limiting step in the biosynthesis of 5-hydroxytryptamine (serotonin) and the first reaction in the synthesis of melatonin. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains (this CD) and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes are regulated in part by the phosphorylation of serine residues N-terminal of the ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153176 [Multi-domain]  Cd Length: 74  Bit Score: 77.21  E-value: 1.07e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 982972215  47 LTLLFALRpTKPPALTRAIKVFETFEAHLHHLETRPAQplRAGSpPLECFVRCEVPGPVVPALLSALRRVAEDVR 121
Cdd:cd04904    1 TSLIFSLK-EEVGALARALKLFEEFGVNLTHIESRPSR--RNGS-EYEFFVDCEVDRGDLDQLISSLRRVVADVN 71
PRK14055 PRK14055
aromatic amino acid hydroxylase; Provisional
197-417 1.28e-16

aromatic amino acid hydroxylase; Provisional


Pssm-ID: 172547 [Multi-domain]  Cd Length: 362  Bit Score: 81.26  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 197 WKEVYSTLRGLYPTHACR---EHLEAFELLERFCGYREdripqledVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVF 273
Cdd:PRK14055 107 WYRLLSSRFSLWKSYCPRfflDYLEAFGLLSDFLDHQA--------VIKFFELETHFSYYPVSGFVAPHQYLSLLQDRYF 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 274 QCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIG---------LASLGVSDEEIEKLST-------LYWF 337
Cdd:PRK14055 179 PIASVMRTLDKDNFSLTPDLIHDLLGHVPWLLHPSFSEFFINMGrlftkviekVQALPSKKQRIQTLQSnliaivrCFWF 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982972215 338 TVEFGLCKQNGEVKAYGAGLLSSYGELLHSLSEEPEIRAFDPDAAAVQPYQDQTYQPVYFVSESFsdakDKLRSYASRIQ 417
Cdd:PRK14055 259 TVESGLIENHEGRKAYGAVLISSPQELGHAFIDNVRVLPLELDQIIRLPFNTSTPQETLFSIRHF----DELVELTSKLE 334
ACT_AAAH-PDT-like cd04880
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ...
48-121 3.73e-09

ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes appear to be regulated, in part, by the phosphorylation of serine residues N-terminal of the ACT domain. Also included in this CD are the C-terminal ACT domains of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme found in plants, fungi, bacteria, and archaea. The P-protein of Escherichia coli (CM-PDT) catalyzes the conversion of chorismate to prephenate and then the decarboxylation and dehydration to form phenylpyruvate. These are the first two steps in the biosynthesis of L-Phe and L-Tyr via the shikimate pathway in microorganisms and plants. The E. coli P-protein (CM-PDT) has three domains with an N-terminal domain with chorismate mutase activity, a middle domain with prephenate dehydratase activity, and an ACT regulatory C-terminal domain. The prephenate dehydratase enzyme has a PDT and ACT domain. The ACT domain is essential to bring about the negative allosteric regulation by L-Phe binding. L-Phe binds with positive cooperativity; with this binding, there is a shift in the protein to less active tetrameric and higher oligomeric forms from a more active dimeric form. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153152 [Multi-domain]  Cd Length: 75  Bit Score: 52.88  E-value: 3.73e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 982972215  48 TLLFALRpTKPPALTRAIKVFETFEAHLHHLETRPAqplRAGSPPLECFVRCEVPG--PVVPALLSALRRVAEDVR 121
Cdd:cd04880    1 SLVFSLK-NKPGALAKALKVFAERGINLTKIESRPS---RKGLWEYEFFVDFEGHIddPDVKEALEELKRVTEDVK 72
 
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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