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Conserved domains on  [gi|14249394|ref|NP_116145|]
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4-hydroxyphenylpyruvate dioxygenase-like protein [Homo sapiens]

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 3.22e-77

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: 236.30  E-value: 3.22e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 158 VSRVDHLTLACTPGSSPTLLRWFHDCLGFCHLPLSPGEDPelglemtaGFGLGGLRLTALQAQPGSIvpTLVLAESLPGa 237
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDI--------GTEYSGLRSIVLANPNETI--KLPLNEPAPG- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 238 tTRQDQVEQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQPGKERQIRAAGHEPHLLARQGILLDGD 317
Cdd:cd07250  70 -KRKSQIQEFLDYHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDGLLVKEDLDTLKELGILVDRD 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14249394 318 KGKFLLQVFTKSLFTEDTFFLELIQRQGATGFGQGNIRALWQSVQE 363
Cdd:cd07250 149 EQGYLLQIFTKPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 9-148 4.18e-35

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: 125.78  E-value: 4.18e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   9 CHIAFHVPAGQPLARNLQRLFGFQPLASR--EVDGWRQLALRSGDAVFLVNEGAGSGEPlYGLDPRHAVPSATNLCFDVA 86
Cdd:cd08342   2 DHVEFYVGNAKQAASYYSTGLGFEPVAYHglETREKASHVLRQGDIRFVFTSPLSSDAP-AADFLAKHGDGVKDVAFRVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14249394  87 DAGAATRELAALGCSVPVPPVRVRDAQGAATYAVVSSPaGILSLTLLERAGYRGPFLPGFRP 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 3.22e-77

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: 236.30  E-value: 3.22e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 158 VSRVDHLTLACTPGSSPTLLRWFHDCLGFCHLPLSPGEDPelglemtaGFGLGGLRLTALQAQPGSIvpTLVLAESLPGa 237
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDI--------GTEYSGLRSIVLANPNETI--KLPLNEPAPG- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 238 tTRQDQVEQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQPGKERQIRAAGHEPHLLARQGILLDGD 317
Cdd:cd07250  70 -KRKSQIQEFLDYHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDGLLVKEDLDTLKELGILVDRD 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14249394 318 KGKFLLQVFTKSLFTEDTFFLELIQRQGATGFGQGNIRALWQSVQE 363
Cdd:cd07250 149 EQGYLLQIFTKPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 10-368 4.35e-57

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: 189.80  E-value: 4.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394    10 HIAFHVPAGQPLARNLQRLFGFQPLA----SREVDGWrqlALRSGDAVFLVNEGAGSGEPLYGLDPRHAvPSATNLCFDV 85
Cdd:TIGR01263   5 FVEFYVGDAKQAARYYFTRLGFEKVAketgHREKAST---VLRQGQINLVLTAPLSPDSPAADFAAKHG-DGVKDVAFRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394    86 ADAGAATRELAALGcSVPVPPVRVRDaqGAATYAVVSSPAGILsLTLLERAGYRGPFLPGFRPVSSA-------PGPGwV 158
Cdd:TIGR01263  81 DDVAAAFEAAVERG-AEPVQAPTEDE--GDVWLATIKGIGDVV-HTLVDRGGYKGSFYPGFFESLLDaalhgppPGVG-L 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   159 SRVDHLTLACTPGSSPTLLRWFHDCLGFchlplspgedPELgLEMTAGFGLGGLRLTALQAQPGSIvpTLVLAEslPGAT 238
Cdd:TIGR01263 156 IAIDHLVGNVERGQMESWAEFYEKIFGF----------REF-RSFDIKTEYSALNSIVMASPDGKV--KIPLNE--PASG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   239 TRQDQVEQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQPGkERQIRAAGHEPHLLARQGILLDGDK 318
Cdd:TIGR01263 221 KDKSQIEEFLEFYNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLG-ERVGGHVKEDLDTLRELNILIDGDE 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14249394   319 GKFLLQVFTKSLFTEDTFFLELIQRQGATGFGQGNIRALWQSV-QEQSARS 368
Cdd:TIGR01263 300 DGYLLQIFTKPLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIeREQERRG 350
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 10-367 4.43e-54

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: 181.24  E-value: 4.43e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  10 HIAFHVPAGQPLARnLQRLFGFQPLA---SREVDGWRQlalrsGDAVFLVNEGAGSgePLYGLDPRHAvPSATNLCFDVA 86
Cdd:COG3185   6 FVEFAVGDAEQLAF-LLEALGFTLVArhrSKAVTLYRQ-----GDINFVLNAEPDS--FAARFAREHG-PGVCAIAFRVD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  87 DAGAATRELAALGCSVPVPPvrvrdAQGAATYAVVSSPAGILsLTLLERAGYRGPFLPGFRPVSSAPGPGWV--SRVDHL 164
Cdd:COG3185  77 DAAAAYERALALGAEPFEGP-----GPGELRIPAIRGIGGSL-HYFVDRYGYGGIYDPDFEPLPGDAAPAGAglTRIDHI 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 165 TLACTPGSSPTLLRWFHDCLGFchlPLSPGEDPELGLemtagfglGGLRLTALQAQPGSIvpTLVLAESlpgaTTRQDQV 244
Cdd:COG3185 151 GIAVPRGDLDEWVLFYEDVLGF---EEIREEDIEDPY--------QGVRSAVLQSPDGKV--RIPLNEP----TSPDSQI 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 245 EQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQpGKERqIRAAGHEPHLLARQGILLDGDKGKFLLQ 324
Cdd:COG3185 214 AEFLEKYRGEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDD-LEPR-VGAHGEDVAFLHPKGILVDRDTGGVLLQ 291

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 14249394 325 VFTKSLFteDTFFLELIQRQGATGFGQGNIRALWQSVQEQSAR 367
Cdd:COG3185 292 IFTKPVG--GTFFFELIQRKGGEGFGEGNFKALFEAIEREQIR 332
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 9-148 4.18e-35

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: 125.78  E-value: 4.18e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   9 CHIAFHVPAGQPLARNLQRLFGFQPLASR--EVDGWRQLALRSGDAVFLVNEGAGSGEPlYGLDPRHAVPSATNLCFDVA 86
Cdd:cd08342   2 DHVEFYVGNAKQAASYYSTGLGFEPVAYHglETREKASHVLRQGDIRFVFTSPLSSDAP-AADFLAKHGDGVKDVAFRVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14249394  87 DAGAATRELAALGCSVPVPPVRVRDAQGAATYAVVSSPaGILSLTLLERAGYRGPFLPGFRP 148
Cdd:cd08342  81 DADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGY-GDVVHTFVDRKGYKGPFLPGFEP 141
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 46-363 2.47e-22

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 97.05  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   46 ALRSGDAVFL------VNEGAG-----SGEPLYGLDPRHAVPSATN-------LCFDVADAGAATRELAALGCSVPVPPV 107
Cdd:PLN02875  43 LLRSGDLVFLftapysPKIGAGdddpaSTAPHPSFSSDAARRFFAKhglavraVGVLVEDAEEAFRTSVAHGARPVLEPT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  108 RVRDAQGAATyAVVSSPA--GILSLTLLERAGYRGP-FLPGFRPVSSAPG--PGW-VSRVDHltlacTPGSSPTLL---R 178
Cdd:PLN02875 123 ELGDEASGGK-AVIAEVElyGDVVLRYVSYKGFDGAkFLPGYEPVESSSSfpLDYgLRRLDH-----AVGNVPNLLpavN 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  179 WFHDCLGFCHLPLSPGEDpeLGlemTAGFGLGGLRLtalqAQPGSIVpTLVLAESLPGaTTRQDQVEQFLARHKGPGLQH 258
Cdd:PLN02875 197 YIAGFTGFHEFAEFTAED--VG---TVDSGLNSMVL----ASNNEMV-LLPLNEPTFG-TKRKSQIQTYLEHNEGPGLQH 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  259 VGLYTPNIV----EATEGVATAGGQFLAPPGA-YYQQ-PGK------ERQIRaaghephLLARQGILLDGDKGKFLLQVF 326
Cdd:PLN02875 266 LALKSDDIFgtlrEMRARSHIGGFEFMPPPPPtYYKNlKKRvgdvltEEQIK-------ECEELGILVDKDDQGVLLQIF 338

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 14249394  327 TKSLFTEDTFFLELIQR----------------QGATGFGQGNIRALWQSVQE 363
Cdd:PLN02875 339 TKPVGDRPTLFLEIIQRigcmekdeegkeyeqaGGCGGFGKGNFSELFKSIEE 391
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-137 9.08e-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: 36.12  E-value: 9.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   7 RLCHIAFHVPAgqpLARNL---QRLFGFQPLASREV--DGWRQLALRSGDAV---FLVNEGAGsgeplygldPRHAVPSA 78
Cdd:COG0346   2 GLHHVTLRVSD---LEASLafyTDVLGLELVKRTDFgdGGFGHAFLRLGDGTeleLFEAPGAA---------PAPGGGGL 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14249394  79 TNLCFDVADAGAATRELAALGCSVPVPPvrvRDAQGAATYAVVSSPAGILsLTLLERAG 137
Cdd:COG0346  70 HHLAFRVDDLDAAYARLRAAGVEIEGEP---RDRAYGYRSAYFRDPDGNL-IELVEPPP 124
 
Name Accession Description Interval E-value
HPPD_C_like cd07250
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ...
 158-363 3.22e-77

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: 236.30  E-value: 3.22e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 158 VSRVDHLTLACTPGSSPTLLRWFHDCLGFCHLPLSPGEDPelglemtaGFGLGGLRLTALQAQPGSIvpTLVLAESLPGa 237
Cdd:cd07250   1 LTRIDHVVGNVPDGEMDPAVEWYEKCLGFHRFWEFDDEDI--------GTEYSGLRSIVLANPNETI--KLPLNEPAPG- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 238 tTRQDQVEQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQPGKERQIRAAGHEPHLLARQGILLDGD 317
Cdd:cd07250  70 -KRKSQIQEFLDYHGGAGVQHIALNTDDIFATVRALRARGVEFLPPPDAYYDDLRERLDGLLVKEDLDTLKELGILVDRD 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 14249394 318 KGKFLLQVFTKSLFTEDTFFLELIQRQGATGFGQGNIRALWQSVQE 363
Cdd:cd07250 149 EQGYLLQIFTKPLQDRPTLFFEIIQRRGAGGFGAGNFKALFEAIER 194
4HPPD TIGR01263
4-hydroxyphenylpyruvate dioxygenase; This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine ...
 10-368 4.35e-57

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: 189.80  E-value: 4.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394    10 HIAFHVPAGQPLARNLQRLFGFQPLA----SREVDGWrqlALRSGDAVFLVNEGAGSGEPLYGLDPRHAvPSATNLCFDV 85
Cdd:TIGR01263   5 FVEFYVGDAKQAARYYFTRLGFEKVAketgHREKAST---VLRQGQINLVLTAPLSPDSPAADFAAKHG-DGVKDVAFRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394    86 ADAGAATRELAALGcSVPVPPVRVRDaqGAATYAVVSSPAGILsLTLLERAGYRGPFLPGFRPVSSA-------PGPGwV 158
Cdd:TIGR01263  81 DDVAAAFEAAVERG-AEPVQAPTEDE--GDVWLATIKGIGDVV-HTLVDRGGYKGSFYPGFFESLLDaalhgppPGVG-L 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   159 SRVDHLTLACTPGSSPTLLRWFHDCLGFchlplspgedPELgLEMTAGFGLGGLRLTALQAQPGSIvpTLVLAEslPGAT 238
Cdd:TIGR01263 156 IAIDHLVGNVERGQMESWAEFYEKIFGF----------REF-RSFDIKTEYSALNSIVMASPDGKV--KIPLNE--PASG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   239 TRQDQVEQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQPGkERQIRAAGHEPHLLARQGILLDGDK 318
Cdd:TIGR01263 221 KDKSQIEEFLEFYNGAGVQHIALNTDDIVRTVRALRARGVEFLDTPDTYYDLLG-ERVGGHVKEDLDTLRELNILIDGDE 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 14249394   319 GKFLLQVFTKSLFTEDTFFLELIQRQGATGFGQGNIRALWQSV-QEQSARS 368
Cdd:TIGR01263 300 DGYLLQIFTKPLQDRGTLFFEIIQRKGAGGFGEGNFKALFEAIeREQERRG 350
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 10-367 4.43e-54

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: 181.24  E-value: 4.43e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  10 HIAFHVPAGQPLARnLQRLFGFQPLA---SREVDGWRQlalrsGDAVFLVNEGAGSgePLYGLDPRHAvPSATNLCFDVA 86
Cdd:COG3185   6 FVEFAVGDAEQLAF-LLEALGFTLVArhrSKAVTLYRQ-----GDINFVLNAEPDS--FAARFAREHG-PGVCAIAFRVD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  87 DAGAATRELAALGCSVPVPPvrvrdAQGAATYAVVSSPAGILsLTLLERAGYRGPFLPGFRPVSSAPGPGWV--SRVDHL 164
Cdd:COG3185  77 DAAAAYERALALGAEPFEGP-----GPGELRIPAIRGIGGSL-HYFVDRYGYGGIYDPDFEPLPGDAAPAGAglTRIDHI 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 165 TLACTPGSSPTLLRWFHDCLGFchlPLSPGEDPELGLemtagfglGGLRLTALQAQPGSIvpTLVLAESlpgaTTRQDQV 244
Cdd:COG3185 151 GIAVPRGDLDEWVLFYEDVLGF---EEIREEDIEDPY--------QGVRSAVLQSPDGKV--RIPLNEP----TSPDSQI 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394 245 EQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQpGKERqIRAAGHEPHLLARQGILLDGDKGKFLLQ 324
Cdd:COG3185 214 AEFLEKYRGEGIQHIAFATDDIEATVAALRARGVRFLDIPDNYYDD-LEPR-VGAHGEDVAFLHPKGILVDRDTGGVLLQ 291

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 14249394 325 VFTKSLFteDTFFLELIQRQGATGFGQGNIRALWQSVQEQSAR 367
Cdd:COG3185 292 IFTKPVG--GTFFFELIQRKGGEGFGEGNFKALFEAIEREQIR 332
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 9-148 4.18e-35

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: 125.78  E-value: 4.18e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   9 CHIAFHVPAGQPLARNLQRLFGFQPLASR--EVDGWRQLALRSGDAVFLVNEGAGSGEPlYGLDPRHAVPSATNLCFDVA 86
Cdd:cd08342   2 DHVEFYVGNAKQAASYYSTGLGFEPVAYHglETREKASHVLRQGDIRFVFTSPLSSDAP-AADFLAKHGDGVKDVAFRVE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14249394  87 DAGAATRELAALGCSVPVPPVRVRDAQGAATYAVVSSPaGILSLTLLERAGYRGPFLPGFRP 148
Cdd:cd08342  81 DADAAYERAVARGAKPVAEPVELSDEGGEVVIAAIQGY-GDVVHTFVDRKGYKGPFLPGFEP 141
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 46-363 2.47e-22

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 97.05  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   46 ALRSGDAVFL------VNEGAG-----SGEPLYGLDPRHAVPSATN-------LCFDVADAGAATRELAALGCSVPVPPV 107
Cdd:PLN02875  43 LLRSGDLVFLftapysPKIGAGdddpaSTAPHPSFSSDAARRFFAKhglavraVGVLVEDAEEAFRTSVAHGARPVLEPT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  108 RVRDAQGAATyAVVSSPA--GILSLTLLERAGYRGP-FLPGFRPVSSAPG--PGW-VSRVDHltlacTPGSSPTLL---R 178
Cdd:PLN02875 123 ELGDEASGGK-AVIAEVElyGDVVLRYVSYKGFDGAkFLPGYEPVESSSSfpLDYgLRRLDH-----AVGNVPNLLpavN 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  179 WFHDCLGFCHLPLSPGEDpeLGlemTAGFGLGGLRLtalqAQPGSIVpTLVLAESLPGaTTRQDQVEQFLARHKGPGLQH 258
Cdd:PLN02875 197 YIAGFTGFHEFAEFTAED--VG---TVDSGLNSMVL----ASNNEMV-LLPLNEPTFG-TKRKSQIQTYLEHNEGPGLQH 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  259 VGLYTPNIV----EATEGVATAGGQFLAPPGA-YYQQ-PGK------ERQIRaaghephLLARQGILLDGDKGKFLLQVF 326
Cdd:PLN02875 266 LALKSDDIFgtlrEMRARSHIGGFEFMPPPPPtYYKNlKKRvgdvltEEQIK-------ECEELGILVDKDDQGVLLQIF 338

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 14249394  327 TKSLFTEDTFFLELIQR----------------QGATGFGQGNIRALWQSVQE 363
Cdd:PLN02875 339 TKPVGDRPTLFLEIIQRigcmekdeegkeyeqaGGCGGFGKGNFSELFKSIEE 391
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 10-128 3.55e-03

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: 37.70  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  10 HIAFHVPAGQPLARNLQRLFGFQPL--------ASREVDGWRQLALRSGDAVF---LVNEGAGSGEPLY---GLDPRHAV 75
Cdd:cd16361   4 HVGITVPDLDAAVEFYTDVLGAEVVyrstplaeGDRGGGEMRAAGFVPGFARAriaMLRLGPGPGIELFeykGPEQRAPV 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394  76 PS-----ATNLCFDVADAGAATRELAALGCSVPVPPVRVRDAQGAATYAVV--SSPAGIL 128
Cdd:cd16361  84 PRnsdvgIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVylRDPWGTL 143
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-137 9.08e-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: 36.12  E-value: 9.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249394   7 RLCHIAFHVPAgqpLARNL---QRLFGFQPLASREV--DGWRQLALRSGDAV---FLVNEGAGsgeplygldPRHAVPSA 78
Cdd:COG0346   2 GLHHVTLRVSD---LEASLafyTDVLGLELVKRTDFgdGGFGHAFLRLGDGTeleLFEAPGAA---------PAPGGGGL 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14249394  79 TNLCFDVADAGAATRELAALGCSVPVPPvrvRDAQGAATYAVVSSPAGILsLTLLERAG 137
Cdd:COG0346  70 HHLAFRVDDLDAAYARLRAAGVEIEGEP---RDRAYGYRSAYFRDPDGNL-IELVEPPP 124
 
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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