NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|947239685|ref|WP_055991956|]
View 

MULTISPECIES: 4-hydroxyphenylpyruvate dioxygenase [Priestia]

Protein Classification

4-hydroxyphenylpyruvate dioxygenase family protein( domain architecture ID 11492165)

4-hydroxyphenylpyruvate dioxygenase (4HPPD) family protein similar to Homo sapiens 4-hydroxyphenylpyruvate dioxygenase that catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism

CATH:  3.10.180.10
EC:  1.13.11.27
Gene Ontology:  GO:0042803|GO:0046872|GO:0003868
SCOP:  4001093

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 22-373 9.56e-170

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: 477.16  E-value: 9.56e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685   22 IHHLELYVGNAKQAAYYYSNAFGFKVKAYrglETGCRDRVSYVLEQGAIRLVVTGSLEETTDIAAFVKLHGEGTKDIALK 101
Cdd:TIGR01263   3 FDFVEFYVGDAKQAARYYFTRLGFEKVAK---ETGHREKASTVLRQGQINLVLTAPLSPDSPAADFAAKHGDGVKDVAFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  102 VSDIEKTYKGAIERGAIAIREPWSEEdenGIVKKAIIGTYGDTVHTLVETVNYKGSFLPGYQSY----ELETGTSSTGIV 177
Cdd:TIGR01263  80 VDDVAAAFEAAVERGAEPVQAPTEDE---GDVWLATIKGIGDVVHTLVDRGGYKGSFYPGFFESlldaALHGPPPGVGLI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  178 GIDHIVGNVEV--MDEWTTYYEKVFGFNVLKHFDdenISTEYSALMSKVMMNGTGRIKFPINEPAEGKRKSQIQEYLDFY 255
Cdd:TIGR01263 157 AIDHLVGNVERgqMESWAEFYEKIFGFREFRSFD---IKTEYSALNSIVMASPDGKVKIPLNEPASGKDKSQIEEFLEFY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  256 KGPGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYYEELSERVG-KIDEDLQKLQELSILVDRDDEGYLLQIFTKPIVD 334
Cdd:TIGR01263 234 NGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLGERVGgHVKEDLDTLRELNILIDGDEDGYLLQIFTKPLQD 313

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 947239685  335 RPTLFIEIIQRKGALGFGDGNFKALFESIEREQERRGNI 373
Cdd:TIGR01263 314 RGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQERRGVL 352
 
Name Accession Description Interval E-value
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 22-373 9.56e-170

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: 477.16  E-value: 9.56e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685   22 IHHLELYVGNAKQAAYYYSNAFGFKVKAYrglETGCRDRVSYVLEQGAIRLVVTGSLEETTDIAAFVKLHGEGTKDIALK 101
Cdd:TIGR01263   3 FDFVEFYVGDAKQAARYYFTRLGFEKVAK---ETGHREKASTVLRQGQINLVLTAPLSPDSPAADFAAKHGDGVKDVAFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  102 VSDIEKTYKGAIERGAIAIREPWSEEdenGIVKKAIIGTYGDTVHTLVETVNYKGSFLPGYQSY----ELETGTSSTGIV 177
Cdd:TIGR01263  80 VDDVAAAFEAAVERGAEPVQAPTEDE---GDVWLATIKGIGDVVHTLVDRGGYKGSFYPGFFESlldaALHGPPPGVGLI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  178 GIDHIVGNVEV--MDEWTTYYEKVFGFNVLKHFDdenISTEYSALMSKVMMNGTGRIKFPINEPAEGKRKSQIQEYLDFY 255
Cdd:TIGR01263 157 AIDHLVGNVERgqMESWAEFYEKIFGFREFRSFD---IKTEYSALNSIVMASPDGKVKIPLNEPASGKDKSQIEEFLEFY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  256 KGPGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYYEELSERVG-KIDEDLQKLQELSILVDRDDEGYLLQIFTKPIVD 334
Cdd:TIGR01263 234 NGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLGERVGgHVKEDLDTLRELNILIDGDEDGYLLQIFTKPLQD 313

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 947239685  335 RPTLFIEIIQRKGALGFGDGNFKALFESIEREQERRGNI 373
Cdd:TIGR01263 314 RGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQERRGVL 352
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 19-370 2.54e-148

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: 422.38  E-value: 2.54e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  19 VQSIHHLELYVGNAKQAAYYySNAFGFKVKAYRgletgcRDRVSYVLEQGAIRLVVTGslEETTDIAAFVKLHGEGTKDI 98
Cdd:COG3185    1 LDGIEFVEFAVGDAEQLAFL-LEALGFTLVARH------RSKAVTLYRQGDINFVLNA--EPDSFAARFAREHGPGVCAI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  99 ALKVSDIEKTYKGAIERGAIAIREPwseedENGIVKKAIIGTYGDTVHTLVETVNYKGSFLPGYQSYELETGTSSTGIVG 178
Cdd:COG3185   72 AFRVDDAAAAYERALALGAEPFEGP-----GPGELRIPAIRGIGGSLHYFVDRYGYGGIYDPDFEPLPGDAAPAGAGLTR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 179 IDHIVGNVEV--MDEWTTYYEKVFGFNVLKHFDdenISTEYSALMSKVMMNGTGRIKFPINEPAEGKrkSQIQEYLDFYK 256
Cdd:COG3185  147 IDHIGIAVPRgdLDEWVLFYEDVLGFEEIREED---IEDPYQGVRSAVLQSPDGKVRIPLNEPTSPD--SQIAEFLEKYR 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 257 GPGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYYEELSERVGKIDEDLQKLQELSILVDRDDEGYLLQIFTKPIVDrp 336
Cdd:COG3185  222 GEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDDLEPRVGAHGEDVAFLHPKGILVDRDTGGVLLQIFTKPVGG-- 299

                        330       340       350
                 ....*....|....*....|....*....|....
gi 947239685 337 TLFIEIIQRKGALGFGDGNFKALFESIEREQERR 370
Cdd:COG3185  300 TFFFELIQRKGGEGFGEGNFKALFEAIEREQIRR 333
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 176-365 2.06e-106

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: 310.64  E-value: 2.06e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 176 IVGIDHIVGNVEV--MDEWTTYYEKVFGFNVLKHFDDENISTEYSALMSKVMMNGTGRIKFPINEPAEGKRKSQIQEYLD 253
Cdd:cd07250    1 LTRIDHVVGNVPDgeMDPAVEWYEKCLGFHRFWEFDDEDIGTEYSGLRSIVLANPNETIKLPLNEPAPGKRKSQIQEFLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 254 FYKGPGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYYEELSERVG--KIDEDLQKLQELSILVDRDDEGYLLQIFTKP 331
Cdd:cd07250   81 YHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDglLVKEDLDTLKELGILVDRDEQGYLLQIFTKP 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 947239685 332 IVDRPTLFIEIIQRKGALGFGDGNFKALFESIER 365
Cdd:cd07250  161 LQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 23-369 4.58e-91

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 278.87  E-value: 4.58e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  23 HHLELYVGNAKQAAYYYSNAFGFKVKAYRGLETGCRDRVSYVLEQGAIRLVVT----GSLEETTDIAA------------ 86
Cdd:PLN02875   2 HHVEFWCGDATNTARRFSWGLGMPLVAKSDLTTGNTTYASYLLRSGDLVFLFTapysPKIGAGDDDPAstaphpsfssda 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  87 ---FVKLHGEGTKDIALKVSDIEKTYKGAIERGAIAIREPWSEEDENGIVKKAI--IGTYGDTVHTLVETVNYKG-SFLP 160
Cdd:PLN02875  82 arrFFAKHGLAVRAVGVLVEDAEEAFRTSVAHGARPVLEPTELGDEASGGKAVIaeVELYGDVVLRYVSYKGFDGaKFLP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 161 GYQSYELETGTSST-GIVGIDHIVGNVEVMDEWTTYYEKVFGFNVLKHFDDENISTEYSALMSKVMMNGTGRIKFPINEP 239
Cdd:PLN02875 162 GYEPVESSSSFPLDyGLRRLDHAVGNVPNLLPAVNYIAGFTGFHEFAEFTAEDVGTVDSGLNSMVLASNNEMVLLPLNEP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 240 AEG-KRKSQIQEYLDFYKGPGVQHLALLTNDIIKTVKALKD----NGVEFLDTP-ATYYEELSERVGKI--DEDLQKLQE 311
Cdd:PLN02875 242 TFGtKRKSQIQTYLEHNEGPGLQHLALKSDDIFGTLREMRArshiGGFEFMPPPpPTYYKNLKKRVGDVltEEQIKECEE 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 947239685 312 LSILVDRDDEGYLLQIFTKPIVDRPTLFIEIIQRKGAL----------------GFGDGNFKALFESIErEQER 369
Cdd:PLN02875 322 LGILVDKDDQGVLLQIFTKPVGDRPTLFLEIIQRIGCMekdeegkeyeqaggcgGFGKGNFSELFKSIE-EYEK 394
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
178-292 6.03e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 73.25  E-value: 6.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  178 GIDHIVGNVEVMDEWTTYYEKVFGFNVLKHFDDEnistEYSALMSKVMMNGTGRIKFPINEPAEGKRKsqiqeyldFYKG 257
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAG----EEGGLRSAFFLAGGRVLELLLNETPPPAAA--------GFGG 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 947239685  258 PGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYY 292
Cdd:pfam00903  69 HHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHG 103
 
Name Accession Description Interval E-value
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 22-373 9.56e-170

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: 477.16  E-value: 9.56e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685   22 IHHLELYVGNAKQAAYYYSNAFGFKVKAYrglETGCRDRVSYVLEQGAIRLVVTGSLEETTDIAAFVKLHGEGTKDIALK 101
Cdd:TIGR01263   3 FDFVEFYVGDAKQAARYYFTRLGFEKVAK---ETGHREKASTVLRQGQINLVLTAPLSPDSPAADFAAKHGDGVKDVAFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  102 VSDIEKTYKGAIERGAIAIREPWSEEdenGIVKKAIIGTYGDTVHTLVETVNYKGSFLPGYQSY----ELETGTSSTGIV 177
Cdd:TIGR01263  80 VDDVAAAFEAAVERGAEPVQAPTEDE---GDVWLATIKGIGDVVHTLVDRGGYKGSFYPGFFESlldaALHGPPPGVGLI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  178 GIDHIVGNVEV--MDEWTTYYEKVFGFNVLKHFDdenISTEYSALMSKVMMNGTGRIKFPINEPAEGKRKSQIQEYLDFY 255
Cdd:TIGR01263 157 AIDHLVGNVERgqMESWAEFYEKIFGFREFRSFD---IKTEYSALNSIVMASPDGKVKIPLNEPASGKDKSQIEEFLEFY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  256 KGPGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYYEELSERVG-KIDEDLQKLQELSILVDRDDEGYLLQIFTKPIVD 334
Cdd:TIGR01263 234 NGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLGERVGgHVKEDLDTLRELNILIDGDEDGYLLQIFTKPLQD 313

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 947239685  335 RPTLFIEIIQRKGALGFGDGNFKALFESIEREQERRGNI 373
Cdd:TIGR01263 314 RGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQERRGVL 352
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 19-370 2.54e-148

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: 422.38  E-value: 2.54e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  19 VQSIHHLELYVGNAKQAAYYySNAFGFKVKAYRgletgcRDRVSYVLEQGAIRLVVTGslEETTDIAAFVKLHGEGTKDI 98
Cdd:COG3185    1 LDGIEFVEFAVGDAEQLAFL-LEALGFTLVARH------RSKAVTLYRQGDINFVLNA--EPDSFAARFAREHGPGVCAI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  99 ALKVSDIEKTYKGAIERGAIAIREPwseedENGIVKKAIIGTYGDTVHTLVETVNYKGSFLPGYQSYELETGTSSTGIVG 178
Cdd:COG3185   72 AFRVDDAAAAYERALALGAEPFEGP-----GPGELRIPAIRGIGGSLHYFVDRYGYGGIYDPDFEPLPGDAAPAGAGLTR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 179 IDHIVGNVEV--MDEWTTYYEKVFGFNVLKHFDdenISTEYSALMSKVMMNGTGRIKFPINEPAEGKrkSQIQEYLDFYK 256
Cdd:COG3185  147 IDHIGIAVPRgdLDEWVLFYEDVLGFEEIREED---IEDPYQGVRSAVLQSPDGKVRIPLNEPTSPD--SQIAEFLEKYR 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 257 GPGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYYEELSERVGKIDEDLQKLQELSILVDRDDEGYLLQIFTKPIVDrp 336
Cdd:COG3185  222 GEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDDLEPRVGAHGEDVAFLHPKGILVDRDTGGVLLQIFTKPVGG-- 299

                        330       340       350
                 ....*....|....*....|....*....|....
gi 947239685 337 TLFIEIIQRKGALGFGDGNFKALFESIEREQERR 370
Cdd:COG3185  300 TFFFELIQRKGGEGFGEGNFKALFEAIEREQIRR 333
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 176-365 2.06e-106

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: 310.64  E-value: 2.06e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 176 IVGIDHIVGNVEV--MDEWTTYYEKVFGFNVLKHFDDENISTEYSALMSKVMMNGTGRIKFPINEPAEGKRKSQIQEYLD 253
Cdd:cd07250    1 LTRIDHVVGNVPDgeMDPAVEWYEKCLGFHRFWEFDDEDIGTEYSGLRSIVLANPNETIKLPLNEPAPGKRKSQIQEFLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 254 FYKGPGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYYEELSERVG--KIDEDLQKLQELSILVDRDDEGYLLQIFTKP 331
Cdd:cd07250   81 YHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDglLVKEDLDTLKELGILVDRDEQGYLLQIFTKP 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 947239685 332 IVDRPTLFIEIIQRKGALGFGDGNFKALFESIER 365
Cdd:cd07250  161 LQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 23-369 4.58e-91

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 278.87  E-value: 4.58e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  23 HHLELYVGNAKQAAYYYSNAFGFKVKAYRGLETGCRDRVSYVLEQGAIRLVVT----GSLEETTDIAA------------ 86
Cdd:PLN02875   2 HHVEFWCGDATNTARRFSWGLGMPLVAKSDLTTGNTTYASYLLRSGDLVFLFTapysPKIGAGDDDPAstaphpsfssda 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  87 ---FVKLHGEGTKDIALKVSDIEKTYKGAIERGAIAIREPWSEEDENGIVKKAI--IGTYGDTVHTLVETVNYKG-SFLP 160
Cdd:PLN02875  82 arrFFAKHGLAVRAVGVLVEDAEEAFRTSVAHGARPVLEPTELGDEASGGKAVIaeVELYGDVVLRYVSYKGFDGaKFLP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 161 GYQSYELETGTSST-GIVGIDHIVGNVEVMDEWTTYYEKVFGFNVLKHFDDENISTEYSALMSKVMMNGTGRIKFPINEP 239
Cdd:PLN02875 162 GYEPVESSSSFPLDyGLRRLDHAVGNVPNLLPAVNYIAGFTGFHEFAEFTAEDVGTVDSGLNSMVLASNNEMVLLPLNEP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 240 AEG-KRKSQIQEYLDFYKGPGVQHLALLTNDIIKTVKALKD----NGVEFLDTP-ATYYEELSERVGKI--DEDLQKLQE 311
Cdd:PLN02875 242 TFGtKRKSQIQTYLEHNEGPGLQHLALKSDDIFGTLREMRArshiGGFEFMPPPpPTYYKNLKKRVGDVltEEQIKECEE 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 947239685 312 LSILVDRDDEGYLLQIFTKPIVDRPTLFIEIIQRKGAL----------------GFGDGNFKALFESIErEQER 369
Cdd:PLN02875 322 LGILVDKDDQGVLLQIFTKPVGDRPTLFLEIIQRIGCMekdeegkeyeqaggcgGFGKGNFSELFKSIE-EYEK 394
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 22-164 4.74e-58

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: 185.11  E-value: 4.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  22 IHHLELYVGNAKQAAYYYSNAFGFKVKAYRGLETgcRDRVSYVLEQGAIRLVVTGSLEETTDIAAFVKLHGEGTKDIALK 101
Cdd:cd08342    1 FDHVEFYVGNAKQAASYYSTGLGFEPVAYHGLET--REKASHVLRQGDIRFVFTSPLSSDAPAADFLAKHGDGVKDVAFR 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 947239685 102 VSDIEKTYKGAIERGAIAIREPWSEEDENGIVKKAIIGTYGDTVHTLVETVNYKGSFLPGYQS 164
Cdd:cd08342   79 VEDADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGYGDVVHTFVDRKGYKGPFLPGFEP 141
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
178-292 6.03e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 73.25  E-value: 6.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  178 GIDHIVGNVEVMDEWTTYYEKVFGFNVLKHFDDEnistEYSALMSKVMMNGTGRIKFPINEPAEGKRKsqiqeyldFYKG 257
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAG----EEGGLRSAFFLAGGRVLELLLNETPPPAAA--------GFGG 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 947239685  258 PGVQHLALLTNDIIKTVKALKDNGVEFLDTPATYY 292
Cdd:pfam00903  69 HHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHG 103
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 179-288 1.10e-06

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 47.19  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 179 IDHIVGNVEVMDEWTTYYEKVFGFNVLKHFDDEnisteySALMSKVMMN-GTGRIKF--PINEPaegkrkSQIQEYLDfY 255
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELE------EQGVRVAFLElGNTQIELlePLGED------SPIAKFLD-K 67

                         90       100       110
                 ....*....|....*....|....*....|...
gi 947239685 256 KGPGVQHLALLTNDIIKTVKALKDNGVEFLDTP 288
Cdd:cd07249   68 KGGGLHHIAFEVDDIDAAVEELKAQGVRLLSEG 100
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 178-288 9.40e-06

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 44.60  E-value: 9.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 178 GIDHI---VGNVEVMDEWttyYEKVFGFNVLKHFDDENISTEYSALMskvmMNGTGRI---KFPINEPAEGkrksqiqey 251
Cdd:COG0346    2 GLHHVtlrVSDLEASLAF---YTDVLGLELVKRTDFGDGGFGHAFLR----LGDGTELelfEAPGAAPAPG--------- 65

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 947239685 252 ldfykGPGVQHLALLTNDIIKTVKALKDNGVEFLDTP 288
Cdd:COG0346   66 -----GGGLHHLAFRVDDLDAAYARLRAAGVEIEGEP 97
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
21-132 1.28e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 41.28  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685   21 SIHHLELYVGNAKQAAYYYSNAFGFKVKAYRGLETGcRDRVSYVLEQGAIRLVVTgSLEETTDIAAFVKLHGEGTkdIAL 100
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE-GGLRSAFFLAGGRVLELL-LNETPPPAAAGFGGHHIAF--IAF 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 947239685  101 KVSDIEKTYKGAIERGAIAIREPWSEEDENGI 132
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVEIVREPGRHGWGGRY 108
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 22-123 2.62e-04

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 40.36  E-value: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  22 IHHLELYVGNAKQAAYYYSNAFGFKVKAYRGLETGCRDRVSYVLEQGAIrLVVTgsleETTDIAAFVKLHGEGTkdIALK 101
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTE-LELF----EAPGAAPAPGGGGLHH--LAFR 75

                         90       100
                 ....*....|....*....|..
gi 947239685 102 VSDIEKTYKGAIERGAIAIREP 123
Cdd:COG0346   76 VDDLDAAYARLRAAGVEIEGEP 97
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 181-284 3.50e-04

vicinal oxygen chelate (VOC) family; 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 is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. 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). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 39.82  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685 181 HIVGNVEVMDEWTTYYEKVFGFNVLKHFDDENIsteysalmskVMMNGTGRIKFPINEPAEGKRKsqiqeyldfyKGPGV 260
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF----------AFLRLGPGLRLALLEGPEPERP----------GGGGL 60

                         90       100
                 ....*....|....*....|....
gi 947239685 261 QHLALLTNDIIKTVKALKDNGVEF 284
Cdd:cd06587   61 FHLAFEVDDVDEVDERLREAGAEG 84
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
180-288 4.23e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 39.57  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  180 DHIVGNVEVMDEWTTYYEKVFGFNVLKHFDDEniSTEYSALMskvMMNGTGRIKFPINEPAEGkrksqiQEYLDFyKGPG 259
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSE--PQNVDLAF---ALLGDGPVEVELIQPLDG------DSPLAR-HGPG 68

                          90       100
                  ....*....|....*....|....*....
gi 947239685  260 VQHLALLTNDIIKTVKALKDNGVEFLDTP 288
Cdd:pfam13669  69 LHHLAYWVDDLDAAVARLLDQGYRVAPKG 97
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 22-150 4.21e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; 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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 36.93  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  22 IHHLELYVGNAKQAAYYYSNAFGFKVKAYRGletgcrdrvsyvlEQGAIRLVVTG---SLEETTDIAAFVKLHGEGTK-D 97
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHE-------------EGEYAEFDTGEtklALFSRKEMARSGGPDRRGSAfE 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 947239685  98 IALKVSDIEKTYKGAIERGAIAIREP----WSEedengivKKAIigtYGDTVHTLVE 150
Cdd:cd07264   68 LGFEVDDVEATVEELVERGAEFVREPankpWGQ-------TVAY---VRDPDGNLIE 114
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 24-117 6.52e-03

vicinal oxygen chelate (VOC) family; 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 is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. 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). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 35.96  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 947239685  24 HLELYVGNAKQAAYYYSNAFGFKVkayrgLETGCRDRVSYVLEQGAIRLVVTGSLEETTDiaafvklHGEGTKDIALKVS 103
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEV-----VSRNEGGGFAFLRLGPGLRLALLEGPEPERP-------GGGGLFHLAFEVD 68

                         90
                 ....*....|....
gi 947239685 104 DIEKTYKGAIERGA 117
Cdd:cd06587   69 DVDEVDERLREAGA 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH