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MULTISPECIES: PKHD-type hydroxylase YbiX [Escherichia]

Protein Classification

PKHD-type hydroxylase( domain architecture ID 10006949)

PKHD-type hydroxylase similar to Escherichia coli YbiX, which belongs to a family of 2-oxoglutarate and Fe(II)-dependent oxygenases that catalyze reactions such as oxidation of an organic substrate using a dioxygen molecule

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PiuC COG3128
Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction ...
2-225 8.05e-150

Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction only];


:

Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 415.31  E-value: 8.05e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   2 MYHIPGVLSPQDVARFREHLEQAEWVDGRVTTGAQGAQVKNNQQVDTRSALYAALQNEVLNAVNQHALFFAAALPRTLST 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902  82 PLFNRYQNNETYGFHVDGAVRSHPQNG-WMRTDLSATLFLSDPESYDGGELVVNDTFGQHRVKLPAGDLVLYPSSSLHCV 160
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGqRVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446912902 161 TPVTRGVRVASFMWIQSMIRDDKKRAMLFELDNNIQSLKSHYGESEEILSLLNLYHNLLREWSEI 225
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
 
Name Accession Description Interval E-value
PiuC COG3128
Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction ...
2-225 8.05e-150

Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction only];


Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 415.31  E-value: 8.05e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   2 MYHIPGVLSPQDVARFREHLEQAEWVDGRVTTGAQGAQVKNNQQVDTRSALYAALQNEVLNAVNQHALFFAAALPRTLST 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902  82 PLFNRYQNNETYGFHVDGAVRSHPQNG-WMRTDLSATLFLSDPESYDGGELVVNDTFGQHRVKLPAGDLVLYPSSSLHCV 160
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGqRVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446912902 161 TPVTRGVRVASFMWIQSMIRDDKKRAMLFELDNNIQSLKSHYGESEEILSLLNLYHNLLREWSEI 225
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
PRK05467 PRK05467
Fe(II)-dependent oxygenase superfamily protein; Provisional
1-225 6.55e-143

Fe(II)-dependent oxygenase superfamily protein; Provisional


Pssm-ID: 235483 [Multi-domain]  Cd Length: 226  Bit Score: 398.05  E-value: 6.55e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   1 MMYHIPGVLSPQDVARFREHLEQAEWVDGRVTTGAQGAQVKNNQQVDTRSALYAALQNEVLNAVNQHALFFAAALPRTLS 80
Cdd:PRK05467   1 MLLHIPDVLSPEEVAQIRELLDAAEWVDGRVTAGAQAAQVKNNQQLPEDSPLARELGNLILDALTRNPLFFSAALPRKIH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902  81 TPLFNRYQNNETYGFHVDGAVRSHPQNG-WMRTDLSATLFLSDPESYDGGELVVNDTFGQHRVKLPAGDLVLYPSSSLHC 159
Cdd:PRK05467  81 PPLFNRYEGGMSYGFHVDNAVRSLPGTGgRVRTDLSATLFLSDPDDYDGGELVIEDTYGEHRVKLPAGDLVLYPSTSLHR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446912902 160 VTPVTRGVRVASFMWIQSMIRDDKKRAMLFELDNNIQSLKSHYGESEEILSLLNLYHNLLREWSEI 225
Cdd:PRK05467 161 VTPVTRGVRVASFFWIQSLVRDDSQRELLFDLDTAIQSLLARHGDSPELDLLTGVYHNLLRRWAEV 226
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
10-176 1.97e-31

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 112.87  E-value: 1.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902    10 SPQDVARFREHLEQAEWVDG---RVTTGAQGAQVKNNQQVDTRSALYAALQNEVLNAVNQHaLFFAAALPRTLSTPLFNR 86
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEvtrGIGNPNETSQYRQSNGTWLELLERDLVIERIRQRLADF-LGLLAGLPLSAEDAQVAR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902    87 YQNNETYGFHVDGAVRShpqngwmRTDLSATLFLSDPEsyDGGELVVNDTFGQ--HRVKLPAGDLVLYPSS---SLHCVT 161
Cdd:smart00702  80 YGPGGHYGPHVDNFLYG-------DRIATFILYLNDVE--EGGELVFPGLRLMvvATVKPKKGDLLFFPSGhgrSLHGVC 150
                          170
                   ....*....|....*
gi 446912902   162 PVTRGVRVASFMWIQ 176
Cdd:smart00702 151 PVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
84-175 1.04e-20

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 82.81  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   84 FNRYQNNETYGFHVDgavRSHPQNGWMRTDLSATLFLSDPESYDGGELVVNDTFGQHRVKLPAGDLVLYPSS--SLHCVT 161
Cdd:pfam13640   3 LARYGDGGFYKPHLD---FFEGAEGGGQRRLTVVLYLNDWEEEEGGELVLYDGDGVEDIKPKKGRLVLFPSSelSLHEVL 79
                          90
                  ....*....|....
gi 446912902  162 PVTRGVRVASFMWI 175
Cdd:pfam13640  80 PVTGGERWSITGWF 93
 
Name Accession Description Interval E-value
PiuC COG3128
Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction ...
2-225 8.05e-150

Predicted 2-oxoglutarate- and Fe(II)-dependent dioxygenase YbiX [General function prediction only];


Pssm-ID: 442362 [Multi-domain]  Cd Length: 225  Bit Score: 415.31  E-value: 8.05e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   2 MYHIPGVLSPQDVARFREHLEQAEWVDGRVTTGAQGAQVKNNQQVDTRSALYAALQNEVLNAVNQHALFFAAALPRTLST 81
Cdd:COG3128    1 LLHIPNVLTPEEVAQIRALLAAAEWVDGRVTAGWQAAQVKNNLQLPEDSPLARELGELVLAALGRNPLFFSAALPLRIFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902  82 PLFNRYQNNETYGFHVDGAVRSHPQNG-WMRTDLSATLFLSDPESYDGGELVVNDTFGQHRVKLPAGDLVLYPSSSLHCV 160
Cdd:COG3128   81 PLFNRYEGGMHYGNHVDNAIRGLPGTGqRVRTDLSFTLFLSDPDEYDGGELVIEDTYGEQSVKLPAGDMVLYPSTSLHRV 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446912902 161 TPVTRGVRVASFMWIQSMIRDDKKRAMLFELDNNIQSLKSHYGESEEILSLLNLYHNLLREWSEI 225
Cdd:COG3128  161 TPVTRGERLASFFWIQSMVRDDAQRELLFDLDQAIQSLRARGGDDPEVDRLTGVYHNLLRMWAEV 225
PRK05467 PRK05467
Fe(II)-dependent oxygenase superfamily protein; Provisional
1-225 6.55e-143

Fe(II)-dependent oxygenase superfamily protein; Provisional


Pssm-ID: 235483 [Multi-domain]  Cd Length: 226  Bit Score: 398.05  E-value: 6.55e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   1 MMYHIPGVLSPQDVARFREHLEQAEWVDGRVTTGAQGAQVKNNQQVDTRSALYAALQNEVLNAVNQHALFFAAALPRTLS 80
Cdd:PRK05467   1 MLLHIPDVLSPEEVAQIRELLDAAEWVDGRVTAGAQAAQVKNNQQLPEDSPLARELGNLILDALTRNPLFFSAALPRKIH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902  81 TPLFNRYQNNETYGFHVDGAVRSHPQNG-WMRTDLSATLFLSDPESYDGGELVVNDTFGQHRVKLPAGDLVLYPSSSLHC 159
Cdd:PRK05467  81 PPLFNRYEGGMSYGFHVDNAVRSLPGTGgRVRTDLSATLFLSDPDDYDGGELVIEDTYGEHRVKLPAGDLVLYPSTSLHR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446912902 160 VTPVTRGVRVASFMWIQSMIRDDKKRAMLFELDNNIQSLKSHYGESEEILSLLNLYHNLLREWSEI 225
Cdd:PRK05467 161 VTPVTRGVRVASFFWIQSLVRDDSQRELLFDLDTAIQSLLARHGDSPELDLLTGVYHNLLRRWAEV 226
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
10-176 1.97e-31

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 112.87  E-value: 1.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902    10 SPQDVARFREHLEQAEWVDG---RVTTGAQGAQVKNNQQVDTRSALYAALQNEVLNAVNQHaLFFAAALPRTLSTPLFNR 86
Cdd:smart00702   1 SPAECQKLLEEAEPLGWRGEvtrGIGNPNETSQYRQSNGTWLELLERDLVIERIRQRLADF-LGLLAGLPLSAEDAQVAR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902    87 YQNNETYGFHVDGAVRShpqngwmRTDLSATLFLSDPEsyDGGELVVNDTFGQ--HRVKLPAGDLVLYPSS---SLHCVT 161
Cdd:smart00702  80 YGPGGHYGPHVDNFLYG-------DRIATFILYLNDVE--EGGELVFPGLRLMvvATVKPKKGDLLFFPSGhgrSLHGVC 150
                          170
                   ....*....|....*
gi 446912902   162 PVTRGVRVASFMWIQ 176
Cdd:smart00702 151 PVTRGSRWAITGWIR 165
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
84-175 1.04e-20

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 82.81  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   84 FNRYQNNETYGFHVDgavRSHPQNGWMRTDLSATLFLSDPESYDGGELVVNDTFGQHRVKLPAGDLVLYPSS--SLHCVT 161
Cdd:pfam13640   3 LARYGDGGFYKPHLD---FFEGAEGGGQRRLTVVLYLNDWEEEEGGELVLYDGDGVEDIKPKKGRLVLFPSSelSLHEVL 79
                          90
                  ....*....|....
gi 446912902  162 PVTRGVRVASFMWI 175
Cdd:pfam13640  80 PVTGGERWSITGWF 93
PKHD_C pfam18331
PKHD-type hydroxylase C-terminal domain; This is the C-terminal domain found in PKHD-type ...
182-224 2.60e-16

PKHD-type hydroxylase C-terminal domain; This is the C-terminal domain found in PKHD-type hydroxylase enzymes. Family members are found mostly in Bacteria and carry the 2OG-Fe(II) oxygenase superfamily pfam13640.


Pssm-ID: 436417 [Multi-domain]  Cd Length: 43  Bit Score: 69.81  E-value: 2.60e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446912902  182 DKKRAMLFELDNNIQSLKSHYGESEEILSLLNLYHNLLREWSE 224
Cdd:pfam18331   1 DAQRRLLFDLDQAIQRLRADLGDDPAVVGLTGVYHNLLRRWAE 43
EGL9 COG3751
Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain ...
4-165 5.50e-05

Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442965 [Multi-domain]  Cd Length: 195  Bit Score: 42.62  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902   4 HIPGVLSPQDVARFREHLEQAEWVD--GRVTTGAQGAQVKNN------------QQVDTRSALYAALQNEVLNAVNQHA- 68
Cdd:COG3751   14 VIDDFLPPELAEALLAELPALDEAGafKPAGIGRGLDHQVNEwirrdsilwldeKLASAAQARYLAALEELREALNSPLf 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446912902  69 --LFFAAALprtlstplFNRYQNNETYGFHVDgavrsHPQNGWMRTdLSATLFLS-DPESYDGGELVVNDTFGQHRVK-- 143
Cdd:COG3751   94 lgLFEYEGH--------FARYPPGGFYKRHLD-----AFRGDLNRR-LSLVLYLNpDWQPEWGGELELYDDDGSEEEVtv 159
                        170       180
                 ....*....|....*....|....
gi 446912902 144 LP-AGDLVLYPSSSL-HCVTPVTR 165
Cdd:COG3751  160 APrFNRLVLFLSEEFpHEVLPVGR 183
 
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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