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Conserved domains on  [gi|22122847|ref|NP_666368|]
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4-hydroxyphenylpyruvate dioxygenase-like protein [Mus musculus]

Protein Classification

4-hydroxyphenylpyruvate dioxygenase-like protein( domain architecture ID 10170046)

4-hydroxyphenylpyruvate dioxygenase-like protein may have dioxygenase activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 158-363 3.72e-72

C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain.


:

Pssm-ID: 319913  Cd Length: 194  Bit Score: 223.20  E-value: 3.72e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 158 VSHVDHLTLACTSGSSPMLMRWFHDCLGFHHLPLSPGEDPemglkvaaGSGRGGLRLTALQTPPNNtvPTLVLAESLPGl 237
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDI--------GTEYSGLRSIVLANPNET--IKLPLNEPAPG- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 238 nSKQDQVEQFLTRHGGPGLQHVGLYTPNIIDASEGMAKAGCRLLTPPEAYYQQPGKEEQILAAGHKPGLLERQGILLDGD 317
Cdd:cd07250  70 -KRKSQIQEFLDYHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDGLLVKEDLDTLKELGILVDRD 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 22122847 318 KDEFLLQVFTKSLFAEDTFFLELIQRQGATGFGQNNIRALWQSVQE 363
Cdd:cd07250 149 EQGYLLQIFTKPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 9-148 1.87e-26

N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of HPP to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_N_like domain represents the N-terminal domain.


:

Pssm-ID: 319930  Cd Length: 141  Bit Score: 102.67  E-value: 1.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   9 CHIAFHVPAGQPLARDLHRVFGFQPLAVR--EAGGWRQLALRSGDAVFLVNEGTGPQEPLYSLDPHHsVPSATNLCFDVE 86
Cdd:cd08342   2 DHVEFYVGNAKQAASYYSTGLGFEPVAYHglETREKASHVLRQGDIRFVFTSPLSSDAPAADFLAKH-GDGVKDVAFRVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22122847  87 DVDGAARALAARGCIMPVPPTRVRDAQGTATYTVLSSPaGNLSLTLLQRAGYRGSFLPGFRP 148
Cdd:cd08342  81 DADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGY-GDVVHTFVDRKGYKGPFLPGFEP 141
 
Name Accession Description Interval E-value
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 158-363 3.72e-72

C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain.


Pssm-ID: 319913  Cd Length: 194  Bit Score: 223.20  E-value: 3.72e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 158 VSHVDHLTLACTSGSSPMLMRWFHDCLGFHHLPLSPGEDPemglkvaaGSGRGGLRLTALQTPPNNtvPTLVLAESLPGl 237
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDI--------GTEYSGLRSIVLANPNET--IKLPLNEPAPG- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 238 nSKQDQVEQFLTRHGGPGLQHVGLYTPNIIDASEGMAKAGCRLLTPPEAYYQQPGKEEQILAAGHKPGLLERQGILLDGD 317
Cdd:cd07250  70 -KRKSQIQEFLDYHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDGLLVKEDLDTLKELGILVDRD 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 22122847 318 KDEFLLQVFTKSLFAEDTFFLELIQRQGATGFGQNNIRALWQSVQE 363
Cdd:cd07250 149 EQGYLLQIFTKPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 10-367 3.93e-51

4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine and phenylalanine catabolite, to homogentisate. Homogentisate can undergo a further non-enzymatic oxidation and polymerization into brown pigments that protect some bacterial species from light. A similar process occurs spontaneously in blood and is hemolytic (see . In some bacterial species, this enzyme has been studied as a hemolysin. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273528 [Multi-domain]  Cd Length: 352  Bit Score: 174.01  E-value: 3.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847    10 HIAFHVPAGQPLARDLHRVFGFQPLAVreAGGWRQLA---LRSGDAVFLVNEGTGPQEPLYSLDPHHSvPSATNLCFDVE 86
Cdd:TIGR01263   5 FVEFYVGDAKQAARYYFTRLGFEKVAK--ETGHREKAstvLRQGQINLVLTAPLSPDSPAADFAAKHG-DGVKDVAFRVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847    87 DVDGAARALAARGcIMPVPPTRVRDaqGTATYTVLSSpAGNLSLTLLQRAGYRGSFLPGFRPLPC-------TPGPGwVS 159
Cdd:TIGR01263  82 DVAAAFEAAVERG-AEPVQAPTEDE--GDVWLATIKG-IGDVVHTLVDRGGYKGSFYPGFFESLLdaalhgpPPGVG-LI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   160 HVDHLTLACTSGSspmlMR----WFHDCLGFHhlplspgedpEMgLKVAAGSGRGGLRLTALqTPPNNTVpTLVLAEslP 235
Cdd:TIGR01263 157 AIDHLVGNVERGQ----MEswaeFYEKIFGFR----------EF-RSFDIKTEYSALNSIVM-ASPDGKV-KIPLNE--P 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   236 GLNSKQDQVEQFLTRHGGPGLQHVGLYTPNIIDASEGMAKAGCRLLTPPEAYYQQpgKEEQI-LAAGHKPGLLERQGILL 314
Cdd:TIGR01263 218 ASGKDKSQIEEFLEFYNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDL--LGERVgGHVKEDLDTLRELNILI 295

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 22122847   315 DGDKDEFLLQVFTKSLFAEDTFFLELIQRQGATGFGQNNIRALWQSVQEEAAR 367
Cdd:TIGR01263 296 DGDEDGYLLQIFTKPLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQER 348
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 10-368 1.95e-45

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 158.51  E-value: 1.95e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  10 HIAFHVPAGQPLARDLHRvFGFQPLAV---REAGGWRQlalrsGDAVFLVNegTGPQEPLYSLDPHHSvPSATNLCFDVE 86
Cdd:COG3185   6 FVEFAVGDAEQLAFLLEA-LGFTLVARhrsKAVTLYRQ-----GDINFVLN--AEPDSFAARFAREHG-PGVCAIAFRVD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  87 DVDGAARALAARGC--IMPVPPTRVRDAqgtATYTVlsspaGNLSLTLLQRAGYRGSFLPGFRPLPC---TPGPGwVSHV 161
Cdd:COG3185  77 DAAAAYERALALGAepFEGPGPGELRIP---AIRGI-----GGSLHYFVDRYGYGGIYDPDFEPLPGdaaPAGAG-LTRI 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 162 DHLTLACTSGSspML--MRWFHDCLGFHHLPLSPGEDPEMGLKVAA-GSGRGGLRLTalqtppnntvptlvLAESLpgln 238
Cdd:COG3185 148 DHIGIAVPRGD--LDewVLFYEDVLGFEEIREEDIEDPYQGVRSAVlQSPDGKVRIP--------------LNEPT---- 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 239 SKQDQVEQFLTRHGGPGLQHVGLYTPNIIDASEGMAKAGCRLLTPPEAYYQQpgKEEQILAAGHKPGLLERQGILLDGDK 318
Cdd:COG3185 208 SPDSQIAEFLEKYRGEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDD--LEPRVGAHGEDVAFLHPKGILVDRDT 285

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22122847 319 DEFLLQVFTKSLFaeDTFFLELIQRQGATGFGQNNIRALWQSVQEEAARA 368
Cdd:COG3185 286 GGVLLQIFTKPVG--GTFFFELIQRKGGEGFGEGNFKALFEAIEREQIRR 333
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 9-148 1.87e-26

N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of HPP to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_N_like domain represents the N-terminal domain.


Pssm-ID: 319930  Cd Length: 141  Bit Score: 102.67  E-value: 1.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   9 CHIAFHVPAGQPLARDLHRVFGFQPLAVR--EAGGWRQLALRSGDAVFLVNEGTGPQEPLYSLDPHHsVPSATNLCFDVE 86
Cdd:cd08342   2 DHVEFYVGNAKQAASYYSTGLGFEPVAYHglETREKASHVLRQGDIRFVFTSPLSSDAPAADFLAKH-GDGVKDVAFRVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22122847  87 DVDGAARALAARGCIMPVPPTRVRDAQGTATYTVLSSPaGNLSLTLLQRAGYRGSFLPGFRP 148
Cdd:cd08342  81 DADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGY-GDVVHTFVDRKGYKGPFLPGFEP 141
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 46-363 3.71e-18

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 85.11  E-value: 3.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   46 ALRSGDAVFL------VNEGTGPQEPLYSLD-PHHSVPSATNLCFD-----------VEDVDGAARALAARGCIMPVPPT 107
Cdd:PLN02875  43 LLRSGDLVFLftapysPKIGAGDDDPASTAPhPSFSSDAARRFFAKhglavravgvlVEDAEEAFRTSVAHGARPVLEPT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  108 RVRDAQgTATYTVLSSPA--GNLSLTLLQRAGYRG-SFLPGFRPLP----CTPGPGwVSHVDHltlacTSGSSPMLM--- 177
Cdd:PLN02875 123 ELGDEA-SGGKAVIAEVElyGDVVLRYVSYKGFDGaKFLPGYEPVEssssFPLDYG-LRRLDH-----AVGNVPNLLpav 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  178 RWFHDCLGFHHLPLSPGEDpemglkvaAGSGRGGLRLTALQTppNNTVPTLVLAESLPGlNSKQDQVEQFLTRHGGPGLQ 257
Cdd:PLN02875 196 NYIAGFTGFHEFAEFTAED--------VGTVDSGLNSMVLAS--NNEMVLLPLNEPTFG-TKRKSQIQTYLEHNEGPGLQ 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  258 HVGLYTPNIIDASEGMAKA----GCRLL-TPPEAYYQQ-PGK------EEQILaaghkpgLLERQGILLDGDKDEFLLQV 325
Cdd:PLN02875 265 HLALKSDDIFGTLREMRARshigGFEFMpPPPPTYYKNlKKRvgdvltEEQIK-------ECEELGILVDKDDQGVLLQI 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22122847  326 FTKSLFAEDTFFLELIQR----------------QGATGFGQNNIRALWQSVQE 363
Cdd:PLN02875 338 FTKPVGDRPTLFLEIIQRigcmekdeegkeyeqaGGCGGFGKGNFSELFKSIEE 391
 
Name Accession Description Interval E-value
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 158-363 3.72e-72

C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain.


Pssm-ID: 319913  Cd Length: 194  Bit Score: 223.20  E-value: 3.72e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 158 VSHVDHLTLACTSGSSPMLMRWFHDCLGFHHLPLSPGEDPemglkvaaGSGRGGLRLTALQTPPNNtvPTLVLAESLPGl 237
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDI--------GTEYSGLRSIVLANPNET--IKLPLNEPAPG- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 238 nSKQDQVEQFLTRHGGPGLQHVGLYTPNIIDASEGMAKAGCRLLTPPEAYYQQPGKEEQILAAGHKPGLLERQGILLDGD 317
Cdd:cd07250  70 -KRKSQIQEFLDYHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDGLLVKEDLDTLKELGILVDRD 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 22122847 318 KDEFLLQVFTKSLFAEDTFFLELIQRQGATGFGQNNIRALWQSVQE 363
Cdd:cd07250 149 EQGYLLQIFTKPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 10-367 3.93e-51

4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine and phenylalanine catabolite, to homogentisate. Homogentisate can undergo a further non-enzymatic oxidation and polymerization into brown pigments that protect some bacterial species from light. A similar process occurs spontaneously in blood and is hemolytic (see . In some bacterial species, this enzyme has been studied as a hemolysin. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273528 [Multi-domain]  Cd Length: 352  Bit Score: 174.01  E-value: 3.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847    10 HIAFHVPAGQPLARDLHRVFGFQPLAVreAGGWRQLA---LRSGDAVFLVNEGTGPQEPLYSLDPHHSvPSATNLCFDVE 86
Cdd:TIGR01263   5 FVEFYVGDAKQAARYYFTRLGFEKVAK--ETGHREKAstvLRQGQINLVLTAPLSPDSPAADFAAKHG-DGVKDVAFRVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847    87 DVDGAARALAARGcIMPVPPTRVRDaqGTATYTVLSSpAGNLSLTLLQRAGYRGSFLPGFRPLPC-------TPGPGwVS 159
Cdd:TIGR01263  82 DVAAAFEAAVERG-AEPVQAPTEDE--GDVWLATIKG-IGDVVHTLVDRGGYKGSFYPGFFESLLdaalhgpPPGVG-LI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   160 HVDHLTLACTSGSspmlMR----WFHDCLGFHhlplspgedpEMgLKVAAGSGRGGLRLTALqTPPNNTVpTLVLAEslP 235
Cdd:TIGR01263 157 AIDHLVGNVERGQ----MEswaeFYEKIFGFR----------EF-RSFDIKTEYSALNSIVM-ASPDGKV-KIPLNE--P 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   236 GLNSKQDQVEQFLTRHGGPGLQHVGLYTPNIIDASEGMAKAGCRLLTPPEAYYQQpgKEEQI-LAAGHKPGLLERQGILL 314
Cdd:TIGR01263 218 ASGKDKSQIEEFLEFYNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDL--LGERVgGHVKEDLDTLRELNILI 295

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 22122847   315 DGDKDEFLLQVFTKSLFAEDTFFLELIQRQGATGFGQNNIRALWQSVQEEAAR 367
Cdd:TIGR01263 296 DGDEDGYLLQIFTKPLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQER 348
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 10-368 1.95e-45

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 158.51  E-value: 1.95e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  10 HIAFHVPAGQPLARDLHRvFGFQPLAV---REAGGWRQlalrsGDAVFLVNegTGPQEPLYSLDPHHSvPSATNLCFDVE 86
Cdd:COG3185   6 FVEFAVGDAEQLAFLLEA-LGFTLVARhrsKAVTLYRQ-----GDINFVLN--AEPDSFAARFAREHG-PGVCAIAFRVD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  87 DVDGAARALAARGC--IMPVPPTRVRDAqgtATYTVlsspaGNLSLTLLQRAGYRGSFLPGFRPLPC---TPGPGwVSHV 161
Cdd:COG3185  77 DAAAAYERALALGAepFEGPGPGELRIP---AIRGI-----GGSLHYFVDRYGYGGIYDPDFEPLPGdaaPAGAG-LTRI 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 162 DHLTLACTSGSspML--MRWFHDCLGFHHLPLSPGEDPEMGLKVAA-GSGRGGLRLTalqtppnntvptlvLAESLpgln 238
Cdd:COG3185 148 DHIGIAVPRGD--LDewVLFYEDVLGFEEIREEDIEDPYQGVRSAVlQSPDGKVRIP--------------LNEPT---- 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 239 SKQDQVEQFLTRHGGPGLQHVGLYTPNIIDASEGMAKAGCRLLTPPEAYYQQpgKEEQILAAGHKPGLLERQGILLDGDK 318
Cdd:COG3185 208 SPDSQIAEFLEKYRGEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDD--LEPRVGAHGEDVAFLHPKGILVDRDT 285

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 22122847 319 DEFLLQVFTKSLFaeDTFFLELIQRQGATGFGQNNIRALWQSVQEEAARA 368
Cdd:COG3185 286 GGVLLQIFTKPVG--GTFFFELIQRKGGEGFGEGNFKALFEAIEREQIRR 333
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 9-148 1.87e-26

N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of HPP to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_N_like domain represents the N-terminal domain.


Pssm-ID: 319930  Cd Length: 141  Bit Score: 102.67  E-value: 1.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   9 CHIAFHVPAGQPLARDLHRVFGFQPLAVR--EAGGWRQLALRSGDAVFLVNEGTGPQEPLYSLDPHHsVPSATNLCFDVE 86
Cdd:cd08342   2 DHVEFYVGNAKQAASYYSTGLGFEPVAYHglETREKASHVLRQGDIRFVFTSPLSSDAPAADFLAKH-GDGVKDVAFRVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22122847  87 DVDGAARALAARGCIMPVPPTRVRDAQGTATYTVLSSPaGNLSLTLLQRAGYRGSFLPGFRP 148
Cdd:cd08342  81 DADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGY-GDVVHTFVDRKGYKGPFLPGFEP 141
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 46-363 3.71e-18

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 85.11  E-value: 3.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847   46 ALRSGDAVFL------VNEGTGPQEPLYSLD-PHHSVPSATNLCFD-----------VEDVDGAARALAARGCIMPVPPT 107
Cdd:PLN02875  43 LLRSGDLVFLftapysPKIGAGDDDPASTAPhPSFSSDAARRFFAKhglavravgvlVEDAEEAFRTSVAHGARPVLEPT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  108 RVRDAQgTATYTVLSSPA--GNLSLTLLQRAGYRG-SFLPGFRPLP----CTPGPGwVSHVDHltlacTSGSSPMLM--- 177
Cdd:PLN02875 123 ELGDEA-SGGKAVIAEVElyGDVVLRYVSYKGFDGaKFLPGYEPVEssssFPLDYG-LRRLDH-----AVGNVPNLLpav 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  178 RWFHDCLGFHHLPLSPGEDpemglkvaAGSGRGGLRLTALQTppNNTVPTLVLAESLPGlNSKQDQVEQFLTRHGGPGLQ 257
Cdd:PLN02875 196 NYIAGFTGFHEFAEFTAED--------VGTVDSGLNSMVLAS--NNEMVLLPLNEPTFG-TKRKSQIQTYLEHNEGPGLQ 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847  258 HVGLYTPNIIDASEGMAKA----GCRLL-TPPEAYYQQ-PGK------EEQILaaghkpgLLERQGILLDGDKDEFLLQV 325
Cdd:PLN02875 265 HLALKSDDIFGTLREMRARshigGFEFMpPPPPTYYKNlKKRvgdvltEEQIK-------ECEELGILVDKDDQGVLLQI 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 22122847  326 FTKSLFAEDTFFLELIQR----------------QGATGFGQNNIRALWQSVQE 363
Cdd:PLN02875 338 FTKPVGDRPTLFLEIIQRigcmekdeegkeyeqaGGCGGFGKGNFSELFKSIEE 391
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 178-293 1.34e-04

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319968  Cd Length: 150  Bit Score: 41.93  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22122847 178 RWFHDCLGFHHL--PLSPGEDPEMGLKVAA---GSGRGGLRLTALQTPPNntvPTLVLAESLpglNSKQDQVEQFLTRHG 252
Cdd:cd16361  17 EFYTDVLGAEVVyrSTPLAEGDRGGGEMRAagfVPGFARARIAMLRLGPG---PGIELFEYK---GPEQRAPVPRNSDVG 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 22122847 253 GpglQHVGLYTPNIIDASEGMAKAGCRLLTPP-EAYYQQPGK 293
Cdd:cd16361  91 I---FHFALQVDDVEAAAERLAAAGGKVLMGPrEIPDGGPGK 129
 
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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