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Conserved domains on  [gi|8393557|ref|NP_058929|]
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4-hydroxyphenylpyruvate dioxygenase [Rattus norvegicus]

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

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List of domain hits

 Name Accession Description Interval E-value
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 19-381 2.97e-168

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: 474.46  E-value: 2.97e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     19 FHSVTFWVGNAKQAASFYCNKMGFEPLAYkglETGSREVVSHVIKQGKIVFVLCSALNPwNKEMGDHLVKHGDGVKDIAF 98
Cdd:TIGR01263   3 FDFVEFYVGDAKQAARYYFTRLGFEKVAK---ETGHREKASTVLRQGQINLVLTAPLSP-DSPAADFAAKHGDGVKDVAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     99 EVEDCEHIVQKARERGAKIVREPWVEEdkfGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPSCNL 178
Cdd:TIGR01263  79 RVDDVAAAFEAAVERGAEPVQAPTEDE---GDVWLATIKGIGDVVHTLVDRGGYKGSFYPGFFESLLDAALHGPPPGVGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    179 EIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDdtqVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVDY 258
Cdd:TIGR01263 156 IAIDHLVGNVERGQMESWAEFYEKIFGFREFRSFD---IKTEYSALNSIVMASPDGKVKIPLNEPASGKDKSQIEEFLEF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    259 NGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTskiQVKENMDVLEELKILVDYDEKGYLLQIFTK 338
Cdd:TIGR01263 233 YNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLGERVGG---HVKEDLDTLRELNILIDGDEDGYLLQIFTK 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 8393557    339 PMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALRGNL 381
Cdd:TIGR01263 310 PLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQERRGVL 352
 
Name Accession Description Interval E-value
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 19-381 2.97e-168

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: 474.46  E-value: 2.97e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     19 FHSVTFWVGNAKQAASFYCNKMGFEPLAYkglETGSREVVSHVIKQGKIVFVLCSALNPwNKEMGDHLVKHGDGVKDIAF 98
Cdd:TIGR01263   3 FDFVEFYVGDAKQAARYYFTRLGFEKVAK---ETGHREKASTVLRQGQINLVLTAPLSP-DSPAADFAAKHGDGVKDVAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     99 EVEDCEHIVQKARERGAKIVREPWVEEdkfGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPSCNL 178
Cdd:TIGR01263  79 RVDDVAAAFEAAVERGAEPVQAPTEDE---GDVWLATIKGIGDVVHTLVDRGGYKGSFYPGFFESLLDAALHGPPPGVGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    179 EIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDdtqVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVDY 258
Cdd:TIGR01263 156 IAIDHLVGNVERGQMESWAEFYEKIFGFREFRSFD---IKTEYSALNSIVMASPDGKVKIPLNEPASGKDKSQIEEFLEF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    259 NGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTskiQVKENMDVLEELKILVDYDEKGYLLQIFTK 338
Cdd:TIGR01263 233 YNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLGERVGG---HVKEDLDTLRELNILIDGDEDGYLLQIFTK 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 8393557    339 PMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALRGNL 381
Cdd:TIGR01263 310 PLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQERRGVL 352
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 178-373 2.13e-119

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: 344.15  E-value: 2.13e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  178 LEIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVD 257
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDIGTEYSGLRSIVLANPNETIKLPLNEPAPGKRKSQIQEFLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  258 YNGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTskIQVKENMDVLEELKILVDYDEKGYLLQIFT 337
Cdd:cd07250  81 YHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDG--LLVKEDLDTLKELGILVDRDEQGYLLQIFT 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 8393557  338 KPMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEE 373
Cdd:cd07250 159 KPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 19-378 1.63e-110

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: 326.85  E-value: 1.63e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   19 FHSVTFWVGNAKQAAsFYCNKMGFEPLAYkgletgSREVVSHVIKQGKIVFVLCSALNPWnkeMGDHLVKHGDGVKDIAF 98
Cdd:COG3185   4 IEFVEFAVGDAEQLA-FLLEALGFTLVAR------HRSKAVTLYRQGDINFVLNAEPDSF---AARFAREHGPGVCAIAF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   99 EVEDCEHIVQKARERGAKIVREPwveedKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEaPTYKDtllPKLPSCNL 178
Cdd:COG3185  74 RVDDAAAAYERALALGAEPFEGP-----GPGELRIPAIRGIGGSLHYFVDRYGYGGIYDPDFE-PLPGD---AAPAGAGL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  179 EIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDdtqVHTEYSSLRSIVVANYEESIKMPINEPApgRKKSQIQEYVDY 258
Cdd:COG3185 145 TRIDHIGIAVPRGDLDEWVLFYEDVLGFEEIREED---IEDPYQGVRSAVLQSPDGKVRIPLNEPT--SPDSQIAEFLEK 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  259 NGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTskiqVKENMDVLEELKILVDYDEKGYLLQIFTK 338
Cdd:COG3185 220 YRGEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDDLEPRVGA----HGEDVAFLHPKGILVDRDTGGVLLQIFTK 295

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 8393557  339 PMQDrpTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALR 378
Cdd:COG3185 296 PVGG--TFFFELIQRKGGEGFGEGNFKALFEAIEREQIRR 333
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 19-373 4.30e-78

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 246.13  E-value: 4.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    19 FHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVSHVIKQGKIVFVLcSAlnPWNKEMGDHLV----------- 87
Cdd:PLN02875   1 FHHVEFWCGDATNTARRFSWGLGMPLVAKSDLTTGNTTYASYLLRSGDLVFLF-TA--PYSPKIGAGDDdpastaphpsf 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    88 ----------KHGDGVKDIAFEVEDCEHIVQKARERGAKIVREPWVEED--KFGKVKFAVLQTYGDTTHTLVEKINYTG- 154
Cdd:PLN02875  78 ssdaarrffaKHGLAVRAVGVLVEDAEEAFRTSVAHGARPVLEPTELGDeaSGGKAVIAEVELYGDVVLRYVSYKGFDGa 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   155 RFLPGFEAptykdtlLPKLPSCNLEI----IDHIVGNQPDqeMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVA 230
Cdd:PLN02875 158 KFLPGYEP-------VESSSSFPLDYglrrLDHAVGNVPN--LLPAVNYIAGFTGFHEFAEFTAEDVGTVDSGLNSMVLA 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   231 NYEESIKMPINEPAPGRK-KSQIQEYVDYNGGAGVQHIALRTEDIITTIRHLRER----GMEFLAVPS-SYYRLLRENL- 303
Cdd:PLN02875 229 SNNEMVLLPLNEPTFGTKrKSQIQTYLEHNEGPGLQHLALKSDDIFGTLREMRARshigGFEFMPPPPpTYYKNLKKRVg 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   304 -KTSKIQVKEnmdvLEELKILVDYDEKGYLLQIFTKPMQDRPTLFLEVIQR-----------HNHQ-----GFGAGNFNS 366
Cdd:PLN02875 309 dVLTEEQIKE----CEELGILVDKDDQGVLLQIFTKPVGDRPTLFLEIIQRigcmekdeegkEYEQaggcgGFGKGNFSE 384


                 ....*..
gi 8393557   367 LFKAFEE 373
Cdd:PLN02875 385 LFKSIEE 391
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
180-301 2.23e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 60.54  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    180 IIDHIVgnQPDQEMESASEWYLKNLQFHRFWSVDdtqvHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQiqeyvdyn 259
Cdd:pfam00903   1 RIDHVA--LRVGDLEKSLDFYTDVLGFKLVEETD----AGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGF-------- 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8393557    260 GGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRE 301
Cdd:pfam00903  67 GGHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRY 108
 
Name Accession Description Interval E-value
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 19-381 2.97e-168

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: 474.46  E-value: 2.97e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     19 FHSVTFWVGNAKQAASFYCNKMGFEPLAYkglETGSREVVSHVIKQGKIVFVLCSALNPwNKEMGDHLVKHGDGVKDIAF 98
Cdd:TIGR01263   3 FDFVEFYVGDAKQAARYYFTRLGFEKVAK---ETGHREKASTVLRQGQINLVLTAPLSP-DSPAADFAAKHGDGVKDVAF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     99 EVEDCEHIVQKARERGAKIVREPWVEEdkfGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPSCNL 178
Cdd:TIGR01263  79 RVDDVAAAFEAAVERGAEPVQAPTEDE---GDVWLATIKGIGDVVHTLVDRGGYKGSFYPGFFESLLDAALHGPPPGVGL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    179 EIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDdtqVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVDY 258
Cdd:TIGR01263 156 IAIDHLVGNVERGQMESWAEFYEKIFGFREFRSFD---IKTEYSALNSIVMASPDGKVKIPLNEPASGKDKSQIEEFLEF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    259 NGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTskiQVKENMDVLEELKILVDYDEKGYLLQIFTK 338
Cdd:TIGR01263 233 YNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLGERVGG---HVKEDLDTLRELNILIDGDEDGYLLQIFTK 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 8393557    339 PMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALRGNL 381
Cdd:TIGR01263 310 PLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIEREQERRGVL 352
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 178-373 2.13e-119

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: 344.15  E-value: 2.13e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  178 LEIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQIQEYVD 257
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDIGTEYSGLRSIVLANPNETIKLPLNEPAPGKRKSQIQEFLD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  258 YNGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTskIQVKENMDVLEELKILVDYDEKGYLLQIFT 337
Cdd:cd07250  81 YHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDG--LLVKEDLDTLKELGILVDRDEQGYLLQIFT 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 8393557  338 KPMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEE 373
Cdd:cd07250 159 KPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 19-378 1.63e-110

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: 326.85  E-value: 1.63e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   19 FHSVTFWVGNAKQAAsFYCNKMGFEPLAYkgletgSREVVSHVIKQGKIVFVLCSALNPWnkeMGDHLVKHGDGVKDIAF 98
Cdd:COG3185   4 IEFVEFAVGDAEQLA-FLLEALGFTLVAR------HRSKAVTLYRQGDINFVLNAEPDSF---AARFAREHGPGVCAIAF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   99 EVEDCEHIVQKARERGAKIVREPwveedKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEaPTYKDtllPKLPSCNL 178
Cdd:COG3185  74 RVDDAAAAYERALALGAEPFEGP-----GPGELRIPAIRGIGGSLHYFVDRYGYGGIYDPDFE-PLPGD---AAPAGAGL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  179 EIIDHIVGNQPDQEMESASEWYLKNLQFHRFWSVDdtqVHTEYSSLRSIVVANYEESIKMPINEPApgRKKSQIQEYVDY 258
Cdd:COG3185 145 TRIDHIGIAVPRGDLDEWVLFYEDVLGFEEIREED---IEDPYQGVRSAVLQSPDGKVRIPLNEPT--SPDSQIAEFLEK 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  259 NGGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRENLKTskiqVKENMDVLEELKILVDYDEKGYLLQIFTK 338
Cdd:COG3185 220 YRGEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDDLEPRVGA----HGEDVAFLHPKGILVDRDTGGVLLQIFTK 295

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 8393557  339 PMQDrpTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALR 378
Cdd:COG3185 296 PVGG--TFFFELIQRKGGEGFGEGNFKALFEAIEREQIRR 333
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 19-373 4.30e-78

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 246.13  E-value: 4.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    19 FHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVSHVIKQGKIVFVLcSAlnPWNKEMGDHLV----------- 87
Cdd:PLN02875   1 FHHVEFWCGDATNTARRFSWGLGMPLVAKSDLTTGNTTYASYLLRSGDLVFLF-TA--PYSPKIGAGDDdpastaphpsf 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    88 ----------KHGDGVKDIAFEVEDCEHIVQKARERGAKIVREPWVEED--KFGKVKFAVLQTYGDTTHTLVEKINYTG- 154
Cdd:PLN02875  78 ssdaarrffaKHGLAVRAVGVLVEDAEEAFRTSVAHGARPVLEPTELGDeaSGGKAVIAEVELYGDVVLRYVSYKGFDGa 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   155 RFLPGFEAptykdtlLPKLPSCNLEI----IDHIVGNQPDqeMESASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVA 230
Cdd:PLN02875 158 KFLPGYEP-------VESSSSFPLDYglrrLDHAVGNVPN--LLPAVNYIAGFTGFHEFAEFTAEDVGTVDSGLNSMVLA 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   231 NYEESIKMPINEPAPGRK-KSQIQEYVDYNGGAGVQHIALRTEDIITTIRHLRER----GMEFLAVPS-SYYRLLRENL- 303
Cdd:PLN02875 229 SNNEMVLLPLNEPTFGTKrKSQIQTYLEHNEGPGLQHLALKSDDIFGTLREMRARshigGFEFMPPPPpTYYKNLKKRVg 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   304 -KTSKIQVKEnmdvLEELKILVDYDEKGYLLQIFTKPMQDRPTLFLEVIQR-----------HNHQ-----GFGAGNFNS 366
Cdd:PLN02875 309 dVLTEEQIKE----CEELGILVDKDDQGVLLQIFTKPVGDRPTLFLEIIQRigcmekdeegkEYEQaggcgGFGKGNFSE 384


                 ....*..
gi 8393557   367 LFKAFEE 373
Cdd:PLN02875 385 LFKSIEE 391
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 19-162 3.45e-74

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: 227.09  E-value: 3.45e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   19 FHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETgsREVVSHVIKQGKIVFVLCSALNPWNKeMGDHLVKHGDGVKDIAF 98
Cdd:cd08342   1 FDHVEFYVGNAKQAASYYSTGLGFEPVAYHGLET--REKASHVLRQGDIRFVFTSPLSSDAP-AADFLAKHGDGVKDVAF 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8393557   99 EVEDCEHIVQKARERGAKIVREPWVEEDKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEA 162
Cdd:cd08342  78 RVEDADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGYGDVVHTFVDRKGYKGPFLPGFEP 141
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
180-301 2.23e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 60.54  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    180 IIDHIVgnQPDQEMESASEWYLKNLQFHRFWSVDdtqvHTEYSSLRSIVVANYEESIKMPINEPAPGRKKSQiqeyvdyn 259
Cdd:pfam00903   1 RIDHVA--LRVGDLEKSLDFYTDVLGFKLVEETD----AGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGF-------- 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8393557    260 GGAGVQHIALRTEDIITTIRHLRERGMEFLAVPSSYYRLLRE 301
Cdd:pfam00903  67 GGHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRY 108
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 18-121 4.85e-09

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: 54.23  E-value: 4.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   18 HFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVsHVIKQGKIVFVLCSALnpwnkemGDHLVKHGDGVKDIA 97
Cdd:COG0346   2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHA-FLRLGDGTELELFEAP-------GAAPAPGGGGLHHLA 73

                        90       100
                ....*....|....*....|....
gi 8393557   98 FEVEDCEHIVQKARERGAKIVREP 121
Cdd:COG0346  74 FRVDDLDAAYARLRAAGVEIEGEP 97
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 21-135 1.43e-07

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: 49.45  E-value: 1.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   21 SVTFWVGNAKQAASFYCNKMGFEPLAYKGletGSREVVSHVIKQGKIVFVlcsalnpwnkEMGDHLVKHGDGVKDIAFEV 100
Cdd:cd06587   1 HVALRVPDLDASVAFYEEVLGFEVVSRNE---GGGFAFLRLGPGLRLALL----------EGPEPERPGGGGLFHLAFEV 67

                        90       100       110
                ....*....|....*....|....*....|....*
gi 8393557  101 EDCEHIVQKARERGAKIVREPWVEEDKFGKVKFAV 135
Cdd:cd06587  68 DDVDEVDERLREAGAEGELVAPPVDDPWGGRSFYF 102
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
26-129 2.08e-07

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 49.08  E-value: 2.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   26 VGNAKQAASFYCNKMGFEPLAykgLETGSREVVSHV-IKQGKIVFVLCSAlnpwnkeMGDHLVKHGDGVkDIAFEVEDCE 104
Cdd:COG2764   8 VDDAEEALEFYEDVFGFEVVF---RMTDPDGKIMHAeLRIGGSVLMLSDA-------PPDSPAAEGNGV-SLSLYVDDVD 76

                        90       100       110
                ....*....|....*....|....*....|....
gi 8393557  105 HIVQKARERGAKIVREPWVEE---------DKFG 129
Cdd:COG2764  77 ALFARLVAAGATVVMPLQDTFwgdrfgmvrDPFG 110
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
18-122 2.82e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 48.98  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     18 HFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSrEVVSHVIKQGKIVFVLCSALNPWNKEMGdhlvKHGDGVKDIA 97
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG-GLRSAFFLAGGRVLELLLNETPPPAAAG----FGGHHIAFIA 75

                          90       100
                  ....*....|....*....|....*
gi 8393557     98 FEVEDCEHIVQKARERGAKIVREPW 122
Cdd:pfam00903  76 FSVDDVDAAYDRLKAAGVEIVREPG 100
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 244-289 3.54e-05

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: 42.95  E-value: 3.54e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 8393557  244 APGRKKSQIQEYVDyNGGAGVQHIALRTEDIITTIRHLRERGMEFL 289
Cdd:cd07249  53 EPLGEDSPIAKFLD-KKGGGLHHIAFEVDDIDAAVEELKAQGVRLL 97
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 21-126 5.11e-05

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: 42.32  E-value: 5.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   21 SVTFWVGNAKQAASFYCNKMGFEPlaykGLETGSREVvsHVIKQGKIVFVLCSalnpwNKEMgDHLVKHGDGVKD--IAF 98
Cdd:cd07264   3 YIVLYVDDFAASLRFYRDVLGLPP----RFLHEEGEY--AEFDTGETKLALFS-----RKEM-ARSGGPDRRGSAfeLGF 70

                        90       100
                ....*....|....*....|....*...
gi 8393557   99 EVEDCEHIVQKARERGAKIVREPWVEED 126
Cdd:cd07264  71 EVDDVEATVEELVERGAEFVREPANKPW 98
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 18-136 9.42e-05

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 41.54  E-value: 9.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   18 HFHSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGsrevvshvikqgkivFVLCSALNPWNKEMGDHLVKHGDGVKDIA 97
Cdd:COG3324   4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD---------------YAEFDTDGGQVGGLMPGAEEPGGPGWLLY 68

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 8393557   98 FEVEDCEHIVQKARERGAKIVREPwVEEDKFGkvKFAVL 136
Cdd:COG3324  69 FAVDDLDAAVARVEAAGGTVLRPP-TDIPPWG--RFAVF 104
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 26-148 3.37e-04

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: 40.25  E-value: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557   26 VGNAKQAASFYCNKMGFEPLAYKgletgsrEVVSHVIKqgkIVFV--------LCSALN---PWNKemgdHLVKHGDGVK 94
Cdd:cd07249   8 VPDLDEALKFYEDVLGVKVSEPE-------ELEEQGVR---VAFLelgntqieLLEPLGedsPIAK----FLDKKGGGLH 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 8393557   95 DIAFEVEDCEHIVQKARERGAKIVREPwVEEDKFGKvKFAVLQTYgDTTHTLVE 148
Cdd:cd07249  74 HIAFEVDDIDAAVEELKAQGVRLLSEG-PRIGAHGK-RVAFLHPK-DTGGVLIE 124
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 181-288 1.77e-03

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 433233  Cd Length: 175  Bit Score: 38.86  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557    181 IDHIVGNQPDqeMESASEWYLKNLQFHrfwsVDDTQVHTEYSSLRSIVVAN--YEESIKMPINEPAPGRKKSQIQEYVDY 258
Cdd:pfam13468   1 LDHVVLAVPD--LDEAAARFARALGFT----VTPGGRHPGMGTANALIMFGdgYLELLAVDPEAPAPPRGRWFGLDRLAD 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 8393557    259 ngGAGVQHIALRTEDIITTIRHLRERGMEF 288
Cdd:pfam13468  75 --GEGLLGWALRTDDIDAVAARLRAAGVEP 102
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 258-292 4.82e-03

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: 36.89  E-value: 4.82e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 8393557  258 YNGGAGVQHIALRTEDIITTIRHLRERGMEFLAVP 292
Cdd:COG0346  63 APGGGGLHHLAFRVDDLDAAYARLRAAGVEIEGEP 97
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
20-133 8.25e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 35.72  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557     20 HSVTFWVGNAKQAASFYCNKMGFEPLAYKGLETGSREVVSHVIKQGKIVFVLCSALNPwnkemGDHLVKHGDGVKDIAFE 99
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVEVELIQPLDG-----DSPLARHGPGLHHLAYW 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 8393557    100 VEDCEHIVQKARERGAKIVREPWVEEDKFGKVKF 133
Cdd:pfam13669  76 VDDLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 183-292 8.66e-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: 8.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393557  183 HIVGNQPDqeMESASEWYLKNLQFHRFWSVDDtqvhteysslRSIVVANYEESIKMPINEPAPGRKksqiqeyvdyNGGA 262
Cdd:cd06587   1 HVALRVPD--LDASVAFYEEVLGFEVVSRNEG----------GGFAFLRLGPGLRLALLEGPEPER----------PGGG 58

                        90       100       110
                ....*....|....*....|....*....|
gi 8393557  263 GVQHIALRTEDIITTIRHLRERGMEFLAVP 292
Cdd:cd06587  59 GLFHLAFEVDDVDEVDERLREAGAEGELVA 88
 
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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