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Conserved domains on  [gi|2023547079|ref|XP_008682530|]
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tryptophan 5-hydroxylase 2 [Ursus maritimus]

Protein Classification

ACT and eu_TrpOH domain-containing protein( domain architecture ID 10289117)

ACT and eu_TrpOH domain-containing protein

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 ...
 218-548 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: 707.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 218 PWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLY 297
Cdd:pfam00351   1 PWFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 298 PTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYT 377
Cdd:pfam00351  81 PTHACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 378 PEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL 457
Cdd:pfam00351 161 PEPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 458 SDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLR 537
Cdd:pfam00351 241 SDKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIK 320

                         330
                  ....*....|.
gi 2023547079 538 SDLNTVCDALN 548
Cdd:pfam00351 321 GDLDILTDALE 331
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 130-203 1.02e-30

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 cd04929:

Pssm-ID: 471857 [Multi-domain]  Cd Length: 74  Bit Score: 114.39  E-value: 1.02e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 130 TAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNP 203
Cdd:cd04929     1 TSVIFSLKNEVGGLAKALKLFQELGINVVHIESRKSKRRSSEFEIFVDCECDQRRLDELVQLLKREVASVNMNT 74
 
Name Accession Description Interval E-value
Biopterin_H pfam00351
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
 218-548 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: 707.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 218 PWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLY 297
Cdd:pfam00351   1 PWFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 298 PTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYT 377
Cdd:pfam00351  81 PTHACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 378 PEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL 457
Cdd:pfam00351 161 PEPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 458 SDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLR 537
Cdd:pfam00351 241 SDKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIK 320

                         330
                  ....*....|.
gi 2023547079 538 SDLNTVCDALN 548
Cdd:pfam00351 321 GDLDILTDALE 331
Trp_5_monoox TIGR01270
tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a ...
 127-551 0e+00

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: 702.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 127 GGKTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSE-VEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPE 205
Cdd:TIGR01270  29 VQRLSIIFSLSNVVGDLSKAIAIFQDRHINILHLESRDSKDGTSKtMDVLVDVELFHYGLQEAMDLLKSGLDVHEVSSPI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 206 NVWTEEEE---------LEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRV 276
Cdd:TIGR01270 109 RPTLIEAQytepgsddaTTGVPWFPKKISDLDKCANRVLMYGSELDADHPGFKDTEYRKRRMMFADLALNYKHGEPIPRV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 277 EYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAG 356
Cdd:TIGR01270 189 EYTEEERKTWGTIYRELRRLYKTHACKEFLDNLPLLEKYCGYREDNIPQLEDVSKFLKAKTGFRLRPVAGYLSARDFLSG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 357 LAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQ- 435
Cdd:TIGR01270 269 LAFRVFHCTQYVRHSADPFYTPEPDTCHELLGHMPLLADPSFAQFSQEIGLASLGASEEDIKKLATLYFFTIEFGLCKQd 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 436 EGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNP 515
Cdd:TIGR01270 349 DEQFKVYGAGLLSSVAELQHALSGSAKIKPFDPDRVCEQECLITTFQNAYFYTRSFEEAKEKMREFTNTIKRPFGVRYNP 428

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2023547079 516 YTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMN 551
Cdd:TIGR01270 429 YTESVEVLKNSKSITLAVNELRSDLNLVAGALHKIS 464
eu_TrpOH cd03346
Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino ...
 218-504 0e+00

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: 611.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 218 PWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLY 297
Cdd:cd03346     1 PWFPKKISDLDKCANRVLMYGSELDADHPGFKDNVYRKRRKYFADVAMNYKHGDPIPRVEYTEEEIKTWGTVYRELNRLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 298 PTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYT 377
Cdd:cd03346    81 PTHACREYLKNLPLLEKHCGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCTQYVRHSSDPFYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 378 PEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL 457
Cdd:cd03346   161 PEPDTCHELLGHVPLLADPSFAQFSQEIGLASLGASDEDIQKLATCYFFTVEFGLCKQDGQLKVYGAGLLSSIGELKHAL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2023547079 458 SDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKS 504
Cdd:cd03346   241 SGEAKVKPFDPKVTCKQECLITTFQEAYFVSESFEEAKEKMREFAKT 287
PhhA COG3186
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];
268-493 3.39e-80

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


Pssm-ID: 442419  Cd Length: 279  Bit Score: 252.81  E-value: 3.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 268 KYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLtkycGYREDNVPQLEDVSVFLKERSGFTVRPVAGY 347
Cdd:COG3186    16 RYTDPQGYIDYTAEEHAVWRRLYRRQVALLPGRACDEYLDGLEKL----GLPADRIPQLDEVNERLKALTGWRVVAVPGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 348 LSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGAS--DEDVQKLATCYF 425
Cdd:COG3186    92 IPPDAFFELLANRRFPVATFIRTPEEIDYLPEPDIFHEVFGHVPLLTNPVFADFLQAYGEAGLKASklDSELALLARLYW 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023547079 426 FTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVK-AFDPKTTC**ECLITTFQEAYFVSESFEE 493
Cdd:COG3186   172 FTVEFGLIGTPEGLRIYGAGILSSPGESEYALESDEPNRiPFDLERVMRTPYRIDIYQPTYFVIDSFDQ 240
phhA PRK11913
phenylalanine 4-monooxygenase; Reviewed
 250-493 1.03e-76

phenylalanine 4-monooxygenase; Reviewed


Pssm-ID: 237020  Cd Length: 275  Bit Score: 243.62  E-value: 1.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 250 DNVYRQRRKYFVDVAMGYKYGQPIprVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLtkycGYREDNVPQLEDV 329
Cdd:PRK11913    1 DAAYRARRDAGMEKAADYTADQPW--IDYTAEEHAIWQTLYERQLALLPGRACDEFLEGLEAL----GLPKDRIPQLDEI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 330 SVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLAS 409
Cdd:PRK11913   75 NRVLQAATGWQVVPVPGLIPFDVFFELLANRRFPVATFIRRPEELDYLQEPDIFHDVFGHVPLLTNPVFADFMQAYGKLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 410 LGASDED-VQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL-SDKACVKAFDPKTTC**ECLITTFQEAYFV 487
Cdd:PRK11913  155 LRASKEGrLEFLARLYWFTVEFGLIRTPGGLRIYGAGILSSPGETLYALeSDSPNRRPFDLERVMRTPYRIDIFQPTYFV 234


                  ....*.
gi 2023547079 488 SESFEE 493
Cdd:PRK11913  235 IDSFEQ 240
ACT_TPH cd04929
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan ...
 130-203 1.02e-30

ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes; ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. 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. Very little is known about the role of the ACT domain in TPH, which appears to be regulated by phosphorylation but not by its substrate or cofactor. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153201 [Multi-domain]  Cd Length: 74  Bit Score: 114.39  E-value: 1.02e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 130 TAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNP 203
Cdd:cd04929     1 TSVIFSLKNEVGGLAKALKLFQELGINVVHIESRKSKRRSSEFEIFVDCECDQRRLDELVQLLKREVASVNMNT 74
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 119-161 4.65e-07

Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439847 [Multi-domain]  Cd Length: 274  Bit Score: 51.64  E-value: 4.65e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2023547079 119 SKSETSPEGG-KTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIE 161
Cdd:COG0077   180 GREPAAPTGAdKTSLVFSLPNRPGALYKALGVFATRGINLTKIE 223
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 130-193 2.59e-03

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 36.52  E-value: 2.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 130 TAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTEfnELIQLLK 193
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE--EVLEALK 62
 
Name Accession Description Interval E-value
Biopterin_H pfam00351
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
 218-548 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: 707.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 218 PWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLY 297
Cdd:pfam00351   1 PWFPRKISDLDKCAHLVLKYGPELDADHPGFTDPVYRKRRKEIADIAFNYKHGDPIPRVEYTEEEIKTWGTVYKKLTSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 298 PTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYT 377
Cdd:pfam00351  81 PTHACREYLENFPLLEKNCGYREDNIPQLEDVSNFLKERTGFTLRPVAGLLSARDFLAGLAFRVFHCTQYIRHHSSPMYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 378 PEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL 457
Cdd:pfam00351 161 PEPDCCHELLGHVPLLADPDFAQFSQEIGLASLGASDEDIEKLATCYWFTVEFGLCKQNGELKAYGAGLLSSFGELEYAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 458 SDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLR 537
Cdd:pfam00351 241 SDKPEYKPFDPEVTAVQKYPITTYQPVYFVAESFEDAKEKLRKFASTIKRPFSVRYNPYTQSVEVLDSKDKLKNLLSQIK 320

                         330
                  ....*....|.
gi 2023547079 538 SDLNTVCDALN 548
Cdd:pfam00351 321 GDLDILTDALE 331
Trp_5_monoox TIGR01270
tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a ...
 127-551 0e+00

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: 702.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 127 GGKTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSE-VEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPE 205
Cdd:TIGR01270  29 VQRLSIIFSLSNVVGDLSKAIAIFQDRHINILHLESRDSKDGTSKtMDVLVDVELFHYGLQEAMDLLKSGLDVHEVSSPI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 206 NVWTEEEE---------LEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRV 276
Cdd:TIGR01270 109 RPTLIEAQytepgsddaTTGVPWFPKKISDLDKCANRVLMYGSELDADHPGFKDTEYRKRRMMFADLALNYKHGEPIPRV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 277 EYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAG 356
Cdd:TIGR01270 189 EYTEEERKTWGTIYRELRRLYKTHACKEFLDNLPLLEKYCGYREDNIPQLEDVSKFLKAKTGFRLRPVAGYLSARDFLSG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 357 LAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQ- 435
Cdd:TIGR01270 269 LAFRVFHCTQYVRHSADPFYTPEPDTCHELLGHMPLLADPSFAQFSQEIGLASLGASEEDIKKLATLYFFTIEFGLCKQd 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 436 EGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNP 515
Cdd:TIGR01270 349 DEQFKVYGAGLLSSVAELQHALSGSAKIKPFDPDRVCEQECLITTFQNAYFYTRSFEEAKEKMREFTNTIKRPFGVRYNP 428

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2023547079 516 YTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMN 551
Cdd:TIGR01270 429 YTESVEVLKNSKSITLAVNELRSDLNLVAGALHKIS 464
eu_TrpOH cd03346
Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino ...
 218-504 0e+00

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: 611.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 218 PWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLY 297
Cdd:cd03346     1 PWFPKKISDLDKCANRVLMYGSELDADHPGFKDNVYRKRRKYFADVAMNYKHGDPIPRVEYTEEEIKTWGTVYRELNRLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 298 PTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYT 377
Cdd:cd03346    81 PTHACREYLKNLPLLEKHCGYREDNIPQLEDVSRFLKERTGFTIRPVAGYLSPRDFLAGLAFRVFHCTQYVRHSSDPFYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 378 PEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL 457
Cdd:cd03346   161 PEPDTCHELLGHVPLLADPSFAQFSQEIGLASLGASDEDIQKLATCYFFTVEFGLCKQDGQLKVYGAGLLSSIGELKHAL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2023547079 458 SDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKS 504
Cdd:cd03346   241 SGEAKVKPFDPKVTCKQECLITTFQEAYFVSESFEEAKEKMREFAKT 287
Phe4hydrox_tetr TIGR01268
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ...
 123-551 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: 601.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 123 TSPEGGKTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDC-ECGKTEFNELIQLLKFQTTIVTl 201
Cdd:TIGR01268  10 VNENIAKTSLIFSLKEEAGALAETLKLFQAHDVNLTHIESRPSKTHPGEYEFFVEFdEASDRKLEGVIEHLRQKAEVTV- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 202 nppeNVWTEE--EELEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYT 279
Cdd:TIGR01268  89 ----NILSRDnkQNKDSVPWFPRKINDIDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAFNYKHGQPIPRVEYT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 280 EEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAY 359
Cdd:TIGR01268 165 DEEIATWRTVFNNLTVLYPTHACQEYNHIFPLLQQNCGFREDNIPQLEDVSQFLQDCTGFTLRPVAGLLSSRDFLAGLAF 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 360 RVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQL 439
Cdd:TIGR01268 245 RVFHSTQYIRHHSKPMYTPEPDICHELLGHVPLFADVEFAQFSQEIGLASLGAPDDYIEKLATLYWFTIEFGLCKQDGEK 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 440 RAYGAGLLSSIGELKHALSDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQS 519
Cdd:TIGR01268 325 KAYGAGLLSSFGELQYCLSDKPEVVDFDPEVTCVTKYPITEFQPLYFLAESFEDAKEKLKSFAATIPRPFSVRYNAYTQR 404

                         410       420       430
                  ....*....|....*....|....*....|..
gi 2023547079 520 IEILKDTRSIENVVQDLRSDLNTVCDALNKMN 551
Cdd:TIGR01268 405 VEILDKKAQLQRLADDIRSEISILQEALGKLN 436
eu_PheOH cd03347
Eukaryotic phenylalanine-4-hydroxylase (eu_PheOH); a member of the biopterin-dependent ...
 218-523 0e+00

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: 547.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 218 PWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLY 297
Cdd:cd03347     1 PWFPRTIQDLDRFANQILSYGAELDADHPGFKDPVYRARRKEFADIAYNYKHGQPIPRVEYTEEEKKTWGTVFRELKSLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 298 PTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYT 377
Cdd:cd03347    81 PTHACYEYNHVFPLLEKNCGFSEDNIPQLEDVSNFLQTCTGFRLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHPSKPMYT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 378 PEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL 457
Cdd:cd03347   161 PEPDICHELLGHVPLFADPSFAQFSQEIGLASLGAPDEYIEKLATVYWFTVEFGLCKQGGSIKAYGAGLLSSFGELQYCL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023547079 458 SDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEIL 523
Cdd:cd03347   241 SDKPELLPFEPEKTAVTKYPITEFQPLYYVAESFEDAKEKLRNFAATIPRPFSVRYNPYTQRIEVL 306
eu_TyrOH cd03345
Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino ...
 219-516 9.44e-179

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: 505.43  E-value: 9.44e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 219 WFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYP 298
Cdd:cd03345     1 WFPRHISELDKCHHLVTKYEPDLDLDHPGFSDKVYRERRKLIAEIAFQYKHGDPIPRVEYTAEEIATWKEVYKTLKDLHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 299 THACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTP 378
Cdd:cd03345    81 THACKEYLDAFQLLEKECGYSEDRIPQLEDVSEFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 379 EPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALS 458
Cdd:cd03345   161 EPDCCHELLGHVPMLADPTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKENGELKAYGAGLLSSYGELLHALS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2023547079 459 DKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPY 516
Cdd:cd03345   241 DEPEHRPFDPAATAVQPYQDQTYQPIYFVSESFSDAKDKLRNYASTMKRPFSVRYDPY 298
Tyr_3_monoox TIGR01269
tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member ...
 102-551 3.92e-171

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: 492.52  E-value: 3.92e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 102 SKANSGKKEDKKSNKGNSKSETSPEGGKTAVVFSLR-NEVGGLVKVLNLFQEKHVNMVHIE---SRKSRRRSSEVEIFVD 177
Cdd:TIGR01269  10 NEKDYGRIHSIIINFHPITHEQDSEAAMQNNQFYIRtKEISSLHRILKYIETFKLNLVHFEtrpTRTLSNADVDYSCLIT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 178 CECGKTEFNELIQLLKFQTTIVTlnppENVWTEEEELEdvPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRR 257
Cdd:TIGR01269  90 LEANEINMSLLIESLRGNSFISG----INLLNNQNVKE--DWFPKHISELDKCQHLLTKFQPDLDTDHPGFHDKVYRQRR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 258 KYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSVFLKERS 337
Cdd:TIGR01269 164 EAIAEIAFQYKYGDPIPEVEYTKEEIETWRLVFTTMKDLHASHACREYIDAFQLLEKYCNYNSESIPQLQTISEFLHRTT 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 338 GFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDV 417
Cdd:TIGR01269 244 GFRLRPVAGLLSARDFLASLAFRVFQCTQYIRHHSSPMHTPEPDCIHELLGHMPMLADRQFAQFSQEIGLASLGASEEEI 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 418 QKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEK 497
Cdd:TIGR01269 324 EKLSTLYWFTVEFGLCKENGETKAYGAGLLSSYGELEHAFSDLSEKRPFNPNDAAVQPYQDQGYQKIYFVTESFEDAKRK 403

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 498 MRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMN 551
Cdd:TIGR01269 404 LRNYINTSGRPFIVRFDPITETVEVLDRFSKRKELLKHVKEEIGQLTTALNHLN 457
arom_aa_hydroxylase cd00361
Biopterin-dependent aromatic amino acid hydroxylase; a family of non-heme, iron(II)-dependent ...
 274-497 2.73e-135

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: 391.92  E-value: 2.73e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 274 PRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLtkycGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPRDF 353
Cdd:cd00361     1 PRVDYTEEEHATWRTLYRRLKKLLPTHACREYLEGLELL----GLPEDRIPQLEDVSEFLKALTGWTLVPVAGLISPRDF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 354 LAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASD-EDVQKLATCYFFTIEFGL 432
Cdd:cd00361    77 FALLAFRVFPVTQYIRHPEEPDYTPEPDIFHELFGHVPLLADPSFADFSQEYGLASLGASDlEEIEKLARLYWFTVEFGL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023547079 433 CKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKEK 497
Cdd:cd00361   157 IKEDGELKAYGAGLLSSYGELQHALSDKPKRIPFDPERVARTPYDITSFQPTYFVIESFEQLKEK 221
PhhA COG3186
Phenylalanine-4-hydroxylase [Amino acid transport and metabolism];
268-493 3.39e-80

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


Pssm-ID: 442419  Cd Length: 279  Bit Score: 252.81  E-value: 3.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 268 KYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLtkycGYREDNVPQLEDVSVFLKERSGFTVRPVAGY 347
Cdd:COG3186    16 RYTDPQGYIDYTAEEHAVWRRLYRRQVALLPGRACDEYLDGLEKL----GLPADRIPQLDEVNERLKALTGWRVVAVPGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 348 LSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGAS--DEDVQKLATCYF 425
Cdd:COG3186    92 IPPDAFFELLANRRFPVATFIRTPEEIDYLPEPDIFHEVFGHVPLLTNPVFADFLQAYGEAGLKASklDSELALLARLYW 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023547079 426 FTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVK-AFDPKTTC**ECLITTFQEAYFVSESFEE 493
Cdd:COG3186   172 FTVEFGLIGTPEGLRIYGAGILSSPGESEYALESDEPNRiPFDLERVMRTPYRIDIYQPTYFVIDSFDQ 240
phhA PRK11913
phenylalanine 4-monooxygenase; Reviewed
 250-493 1.03e-76

phenylalanine 4-monooxygenase; Reviewed


Pssm-ID: 237020  Cd Length: 275  Bit Score: 243.62  E-value: 1.03e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 250 DNVYRQRRKYFVDVAMGYKYGQPIprVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLtkycGYREDNVPQLEDV 329
Cdd:PRK11913    1 DAAYRARRDAGMEKAADYTADQPW--IDYTAEEHAIWQTLYERQLALLPGRACDEFLEGLEAL----GLPKDRIPQLDEI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 330 SVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLAS 409
Cdd:PRK11913   75 NRVLQAATGWQVVPVPGLIPFDVFFELLANRRFPVATFIRRPEELDYLQEPDIFHDVFGHVPLLTNPVFADFMQAYGKLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 410 LGASDED-VQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHAL-SDKACVKAFDPKTTC**ECLITTFQEAYFV 487
Cdd:PRK11913  155 LRASKEGrLEFLARLYWFTVEFGLIRTPGGLRIYGAGILSSPGETLYALeSDSPNRRPFDLERVMRTPYRIDIFQPTYFV 234


                  ....*.
gi 2023547079 488 SESFEE 493
Cdd:PRK11913  235 IDSFEQ 240
pro_PheOH cd03348
Prokaryotic phenylalanine-4-hydroxylase (pro_PheOH); a member of the biopterin-dependent ...
 268-493 4.44e-61

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: 201.34  E-value: 4.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 268 KYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLtkycGYREDNVPQLEDVSVFLKERSGFTVRPVAGY 347
Cdd:cd03348     1 DVPDEQGQIDYTPEEHAVWRTLYERQAKLLPGRACDAFLEGLEKL----GLPTDRIPDFADVSERLKAATGWTVVAVPGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 348 LSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGAS-DEDVQKLATCYFF 426
Cdd:cd03348    77 IPDDEFFEHLANRRFPVTNFIRRPEELDYLQEPDIFHDIFGHVPMLTNPVFADFMQAYGKGGLKATgLEDRALLARLYWY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023547079 427 TIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKAC-VKAFDPKTTC**ECLITTFQEAYFVSESFEE 493
Cdd:cd03348   157 TVEFGLIQEPGGLRIYGAGILSSPGETLYALESPDPnRIPFDLERVMRTPYRIDSFQPTYFVIDSFEQ 224
Phe4hydrox_mono TIGR01267
phenylalanine-4-hydroxylase, monomeric form; This model describes the smaller, monomeric form ...
 272-493 1.04e-40

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: 147.71  E-value: 1.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 272 PIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLtkycGYREDNVPQLEDVSVFLKERSGFTVRPVAGYLSPR 351
Cdd:TIGR01267   5 DQGFDHYSEEEHAVWNTLITRQLKLIEGRACQEYLDGIEQL----GLPHDRIPDFDEINRKLQATTGWRIAAVPGLIPFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 352 DFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDED-VQKLATCYFFTIEF 430
Cdd:TIGR01267  81 TFFEHLANRRFPVTTWLRTPEELDYLQEPDIFHDIFGHVPLLTNPVFADFTHTYGKLGLKASALGrVEMLARLYWYTIEF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 431 GLCKQEGQLRAYGAGLLSSIGELKHAL-SDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEE 493
Cdd:TIGR01267 161 GLVETDQGKRIYGAGILSSPKETVYSLeSDEPLHVAFDLLEAMRTPYRIDIFQPLYFVLPSFKR 224
ACT_TPH cd04929
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan ...
 130-203 1.02e-30

ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes; ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. 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. Very little is known about the role of the ACT domain in TPH, which appears to be regulated by phosphorylation but not by its substrate or cofactor. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153201 [Multi-domain]  Cd Length: 74  Bit Score: 114.39  E-value: 1.02e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 130 TAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNP 203
Cdd:cd04929     1 TSVIFSLKNEVGGLAKALKLFQELGINVVHIESRKSKRRSSEFEIFVDCECDQRRLDELVQLLKREVASVNMNT 74
ACT_AAAH cd04904
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ...
 130-203 4.30e-23

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: 93.01  E-value: 4.30e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 130 TAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNP 203
Cdd:cd04904     1 TSLIFSLKEEVGALARALKLFEEFGVNLTHIESRPSRRNGSEYEFFVDCEVDRGDLDQLISSLRRVVADVNILS 74
PRK14056 PRK14056
aromatic amino acid hydroxylase;
277-503 3.63e-19

aromatic amino acid hydroxylase;


Pssm-ID: 237598  Cd Length: 578  Bit Score: 90.89  E-value: 3.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 277 EYTEEETKTWGVVFRELSKLYPTHACREYLKNFplltKYCGYREDNVPQLEDVSVFLKeRSGFTVRPVAGYLSPRDFLAG 356
Cdd:PRK14056   20 QYTPVDHAVWRYVMRQNHSFLKDVAHPAYLNGL----QSTGINIERIPKVEEMNECLA-EIGWGAVAVDGFIPPVAFFEF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 357 LAYRVFHCTQYVRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQ---EIGLASL----------------------G 411
Cdd:PRK14056   95 QGHGVLPIATDIRKVENIEYTPAPDIIHEAAGHAPILADPTYAEYLRrfgEIGAKAIsskedhdvfeavrtlsivkespT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 412 ASDEDV--------------------QKLATCYFFTIEFGLCkqeGQL---RAYGAGLLSSIGELKHALSDK-------- 460
Cdd:PRK14056  175 STPEEVaaaenrviekqnlvsglseaEQISRLFWWTVEYGLI---GTLdnpKIYGAGLLSSVGESKHCLTDAvekvpfsi 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2023547079 461 -ACVK-AFDpkttc**eclITTFQEAYFVSESFEEAKEKMRDFAK 503
Cdd:PRK14056  252 eACTStTYD----------ITKMQPQLFVCPDFEELSEVLEEFAE 286
PRK14055 PRK14055
aromatic amino acid hydroxylase; Provisional
 304-496 1.67e-16

aromatic amino acid hydroxylase; Provisional


Pssm-ID: 172547 [Multi-domain]  Cd Length: 362  Bit Score: 81.26  E-value: 1.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 304 EYLKNFPLLTKYCGYREdnvpqledVSVFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYVRHGSDPLYTPEPDTC 383
Cdd:PRK14055  128 DYLEAFGLLSDFLDHQA--------VIKFFELETHFSYYPVSGFVAPHQYLSLLQDRYFPIASVMRTLDKDNFSLTPDLI 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023547079 384 HELLGHVPLLADPKFAQFSQEIG---------LASLGASDEDVQKLAT-------CYFFTIEFGLCKQEGQLRAYGAGLL 447
Cdd:PRK14055  200 HDLLGHVPWLLHPSFSEFFINMGrlftkviekVQALPSKKQRIQTLQSnliaivrCFWFTVESGLIENHEGRKAYGAVLI 279

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2023547079 448 SSIGELKHALSDKACVKAFDPKTTC**ECLITTFQEAYFVSESFEEAKE 496
Cdd:PRK14055  280 SSPQELGHAFIDNVRVLPLELDQIIRLPFNTSTPQETLFSIRHFDELVE 328
ACT_AAAH-PDT-like cd04880
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH); ACT domain ...
 132-201 1.42e-12

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: 62.90  E-value: 1.42e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023547079 132 VVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTE--FNELIQLLKFQTTIVTL 201
Cdd:cd04880     2 LVFSLKNKPGALAKALKVFAERGINLTKIESRPSRKGLWEYEFFVDFEGHIDDpdVKEALEELKRVTEDVKV 73
ACT_PAH cd04931
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, phenylalanine ...
 122-176 2.75e-09

ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, phenylalanine hydroxylases (PAH); ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, phenylalanine hydroxylases (PAH). PAH catalyzes the hydroxylation of L-Phe to L-Tyr, the first step in the catabolic degradation of L-Phe. In PAH, an autoregulatory sequence, N-terminal of the ACT domain, extends across the catalytic domain active site and regulates the enzyme by intrasteric regulation. It appears that the activation by L-Phe induces a conformational change that converts the enzyme to a high-affinity and high-activity state. Modulation of activity is achieved through inhibition by BH4 and activation by phosphorylation of serine residues of the autoregulatory region. The molecular basis for the cooperative activation process is not fully understood yet. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153203 [Multi-domain]  Cd Length: 90  Bit Score: 54.05  E-value: 2.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2023547079 122 ETSPEGGKTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFV 176
Cdd:cd04931     7 ENSNKNGVISLIFSLKEEVGALAKVLRLFEEKDINLTHIESRPSRLNKDEYEFFI 61
PheA2 COG0077
Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part ...
 119-161 4.65e-07

Prephenate dehydratase [Amino acid transport and metabolism]; Prephenate dehydratase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439847 [Multi-domain]  Cd Length: 274  Bit Score: 51.64  E-value: 4.65e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2023547079 119 SKSETSPEGG-KTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIE 161
Cdd:COG0077   180 GREPAAPTGAdKTSLVFSLPNRPGALYKALGVFATRGINLTKIE 223
ACT_TH cd04930
ACT domain of the nonheme iron-dependent aromatic amino acid hydroxylase, tyrosine ...
 120-193 7.64e-06

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: 45.08  E-value: 7.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 120 KSETSPEGGKTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLK 193
Cdd:cd04930    32 EKEGKAVPQKATLLFSLKEGFSSLSRILKVFETFEAKIHHLESRPSRKEGGDLEVLVRCEVHRSDLLQLISSLR 105
ACT_CM-PDT cd04905
C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) ...
 129-161 5.27e-05

C-terminal ACT domain of the bifunctional chorismate mutase-prephenate dehydratase (CM-PDT) enzyme and the prephenate dehydratase (PDT) enzyme; The C-terminal ACT domain 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 E. coli (CM-PDT, PheA) 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: 153177 [Multi-domain]  Cd Length: 80  Bit Score: 41.72  E-value: 5.27e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2023547079 129 KTAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIE 161
Cdd:cd04905     1 KTSIVFTLPNKPGALYDVLGVFAERGINLTKIE 33
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 130-193 2.59e-03

ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 36.52  E-value: 2.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2023547079 130 TAVVFSLRNEVGGLVKVLNLFQEKHVNMVHIESRKSRRRSSEVEIFVDCECGKTEfnELIQLLK 193
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLE--EVLEALK 62
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 132-193 3.88e-03

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.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 35.73  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023547079 132 VVFSLRNEVGGLVKVLNLFQEKHVNMVHIEsRKSRRRSSEVEIFVDCEcGKTEFNELIQLLK 193
Cdd:cd02116     1 LTVSGPDRPGLLAKVLSVLAEAGINITSIE-QRTSGDGGEADIFIVVD-GDGDLEKLLEALE 60
 
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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