| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20006630m |
| Family | AA2 |
| Protein Properties | Length: 711 Molecular Weight: 77223.9 Isoelectric Point: 5.3261 |
| Chromosome | Chromosome/Scaffold: 7 Start: 2288577 End: 2295121 |
| Description | thylakoidal ascorbate peroxidase |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA2 | 86 | 187 | 1.4e-25 |
| FGNYGPLMIRMAWHCAGSYRTSDGRGGCDGARQRFDPERSWADNTSLDKARKLLWPIKEKYGSALSWGDLMILAGNTAIESMGGPILGFCAGRIDDADGS AS | |||
| AA2 | 472 | 696 | 4.8e-27 |
| LAYQCACSFRQTDYTGGCNGARIRFSPQKDWPNNVAMDRVLAVLEPIKASFPTLTYSDLIVLAGSNALTDAKAKGIRFCPGRSDADPNEPPAPVYPPRTM NNKIAQLMDNGIVMGLDMREMVAIQARLRSPSQQRRLGFSGSWTNDASKLTNEYFRVLLDNDWVNVTSSAGQLEMKAVGKEGIYMTPTDLAIKWDAVLSA IAQEFATDATAFYTAFASAWNKMMI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 711 Download |
| MAAPRFLCAV LISILATQAI QVAAKCPFHF GRARMDDDVG AILQAEPRRM LTSADVKAVN 60 ELNLDAVKAD LKALFLDSKD WWPADFGNYG PLMIRMAWHC AGSYRTSDGR GGCDGARQRF 120 DPERSWADNT SLDKARKLLW PIKEKYGSAL SWGDLMILAG NTAIESMGGP ILGFCAGRID 180 DADGSASEPL GPSLDQEMVA PCSVNGECEA PLGASTMELI YVNPEGPLGN PVPELSAPQI 240 RDIFGRMAMN DSETVALVGG GHAFGKCHGA CPTGPGPSPR QQPWDPWPGT CGNGTMKGKG 300 ENTFTSGFDG PWTTQPTKWD NEYYQNLLKY DWEVYMGPGG HHQWRPVKKD PSDPEELPDI 360 IMLTADVALT RDPAYLEIVK LYASDLGALE RAFSHAWYKL TTRDMGPYTR CLGSQVPPPQ 420 PFQAPLPPPP ATLPDFKAVS KAIAKALRTA SPALEGDLVG GKPYYGALFA NLAYQCACSF 480 RQTDYTGGCN GARIRFSPQK DWPNNVAMDR VLAVLEPIKA SFPTLTYSDL IVLAGSNALT 540 DAKAKGIRFC PGRSDADPNE PPAPVYPPRT MNNKIAQLMD NGIVMGLDMR EMVAIQARLR 600 SPSQQRRLGF SGSWTNDASK LTNEYFRVLL DNDWVNVTSS AGQLEMKAVG KEGIYMTPTD 660 LAIKWDAVLS AIAQEFATDA TAFYTAFASA WNKMMIADRF KGPTANECPS * 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00649 | catalase_peroxidase_1 | 0.0003 | 609 | 703 | 115 | + N-terminal catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear. | ||
| cd00649 | catalase_peroxidase_1 | 1.0e-12 | 435 | 556 | 126 | + N-terminal catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear. | ||
| cd00649 | catalase_peroxidase_1 | 3.0e-158 | 57 | 416 | 376 | + N-terminal catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear. | ||
| COG0376 | KatG | 2.0e-175 | 23 | 700 | 747 | + Catalase (peroxidase I) [Inorganic ion transport and metabolism] | ||
| PRK15061 | PRK15061 | 0 | 57 | 700 | 718 | + catalase/hydroperoxidase HPI(I); Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004601 | peroxidase activity |
| GO:0006979 | response to oxidative stress |
| GO:0020037 | heme binding |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEY53486.1 | 0 | 7 | 700 | 8 | 685 | catalase-peroxidase, putative [Phytophthora infestans T30-4] |
| GenBank | EEY69350.1 | 0 | 55 | 701 | 30 | 632 | catalase-peroxidase, putative [Phytophthora infestans T30-4] |
| GenBank | EEY69351.1 | 0 | 23 | 701 | 21 | 656 | catalase-peroxidase, putative [Phytophthora infestans T30-4] |
| RefSeq | XP_002186090.1 | 0 | 57 | 700 | 49 | 733 | catalase-peroxidase [Phaeodactylum tricornutum CCAP 1055/1] |
| RefSeq | YP_325577.1 | 0 | 61 | 700 | 65 | 731 | EHEC-catalase/peroxidase [Escherichia coli O157:H7 EDL933] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1itk_B | 0 | 57 | 700 | 54 | 728 | A Chain A, Crystal Structure Of Catalase-peroxidase From Haloarcula Marismortui |
| PDB | 1itk_A | 0 | 57 | 700 | 54 | 728 | A Chain A, Crystal Structure Of Catalase-peroxidase From Haloarcula Marismortui |
| PDB | 3uw8_B | 0 | 57 | 700 | 54 | 728 | A Chain A, Crystal Structure Analysis Of The Ser305thr Variants Of Katg From Haloarcula Marismortui |
| PDB | 3uw8_A | 0 | 57 | 700 | 54 | 728 | A Chain A, Crystal Structure Analysis Of The Ser305thr Variants Of Katg From Haloarcula Marismortui |
| PDB | 3vll_B | 0 | 57 | 700 | 54 | 728 | A Chain A, Crystal Structure Analysis Of The Ser305thr Variants Of Katg From Haloarcula Marismortui |
