|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
DOI=10.1038/37052; PubMed=9389475 [NCBI, ExPASy, EBI, Israel, Japan]
Klenk H.-P.,
Clayton R.A.,
Tomb J.-F.,
White O.,
Nelson K.E.,
Ketchum K.A.,
Dodson R.J.,
Gwinn M.L.,
Hickey E.K.,
Peterson J.D.,
Richardson D.L.,
Kerlavage A.R.,
Graham D.E.,
Kyrpides N.C.,
Fleischmann R.D.,
Quackenbush J.,
Lee N.H.,
Sutton G.G.,
Gill S.R., ![]()
Kirkness E.F.,
Dougherty B.A.,
McKenney K.,
Adams M.D.,
Loftus B.J.,
Peterson S.N.,
Reich C.I.,
McNeil L.K.,
Badger J.H.,
Glodek A.,
Zhou L.,
Overbeek R.,
Gocayne J.D.,
Weidman J.F.,
McDonald L.A.,
Utterback T.R.,
Cotton M.D.,
Spriggs T.,
Artiach P.,
Kaine B.P.,
Sykes S.M.,
Sadow P.W.,
D'Andrea K.P.,
Bowman C.,
Fujii C.,
Garland S.A.,
Mason T.M.,
Olsen G.J.,
Fraser C.M.,
Smith H.O.,
Woese C.R.,
Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
|
[2]
|
BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1016/j.abb.2007.12.008; PubMed=18178143 [NCBI, ExPASy, EBI, Israel, Japan]
Singh R.,
Wiseman B.,
Deemagarn T.,
Jha V.,
Switala J.,
Loewen P.C.;
"Comparative study of catalase-peroxidases (KatGs).";
Arch. Biochem. Biophys. 471:207-214(2008).
|
|
|
|
- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity.
- CATALYTIC ACTIVITY: 2 H2O2 = O2 + 2 H2O.
- CATALYTIC ACTIVITY: Donor + H2O2 = oxidized donor + 2 H2O.
- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer (By similarity).
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=32 mM for H2O2 for the catalase reaction (at pH 5.5-6.0); | | KM=3.8 mM for H2O2 for the catalase reaction (at pH 7.0); | | KM=95 mM for H2O2 for the peroxidase reaction; | | KM=16 mM for ABTS for the peroxidase reaction; | | Vmax=11760 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0); | | Vmax=5500 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0); | | Vmax=12 µmol/min/mg enzyme for ABTS for the peroxidase reaction; | | pH dependence: |
Optimum pH is 4.5 for the peroxidase reaction; | |
- SUBUNIT: Homodimer or homotetramer (By similarity).
- PTM: The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme (By similarity).
- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 741 AA [This is the length of the unprocessed precursor] |
Molecular weight: 84854 Da [This is the MW of the unprocessed precursor] |
CRC64: A931DF34F050FC63 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MMRQGGVMVG ARKRWITDWW PNRLNLKILR QNLQNPYGED YDYVEEVENL DIDAVIRDLK
70 80 90 100 110 120
ELMRSSQDWW PADFGHYGPL FIRLAWHSAG SYRIFDGRGG ARDGSIRFPP RINWPDNINL
130 140 150 160 170 180
DKAIRLLWPI KKKYGRKLSW ADLIILAGTV AMEDMGVKLF GFALGREDIF EPDESPDWGP
190 200 210 220 230 240
EEEMLTAKRG EKEELERPFA ATEMGLIYVN PEGPGGNPDP LGSAQEIRVA FRRMGMNDEE
250 260 270 280 290 300
TVALIAGGHA FGKCHGAGPA DYLGPDPSSS PIEMQGLGWK YNYGKGKGSD TFTSGLEVTW
310 320 330 340 350 360
SPTPTKFGIN YLRILFTYEW ELEKSPAGKN QWVAKDAPEI IPDAHDPNKK HRPRMLTADL
370 380 390 400 410 420
ALRFDPEFSK IARRFLENPE EFEKAFAIAW YKLTHRDMGP KDCYIGKYVP EETFVWQDPL
430 440 450 460 470 480
PRRDYELVDE KDVEELKRRI LASGLSLSQL VYFAWASAST YRNSDRRGGA NGARIRLKPM
490 500 510 520 530 540
SVWEVNHPEE LKKVIAAYEK IQQEFNEGAK GSEKRISIAD LIVLGGIAAV EEAARRAGFS
550 560 570 580 590 600
VKVPFIPGRV DAQQEHVDEE FYRVIEPFAD GFRNYFRYPE RINERDVYTT PEYFLVDKAN
610 620 630 640 650 660
LLTLTVPEMV VLIGGMRALG ANYSHSDYGV LTERPGVLSN DFFVNLLDMS VEWRAADDYR
670 680 690 700 710 720
YTFEGYDRKS GELRWRATRV DLILGHHDEL RAVAEVYGCD DAKEKFVKDF AAVCAKVMHL
730 740
DRFDLWRSNR KLYKEITAGL R
|
O28050 in FASTA format |
|
ExPASy Home page
YPRC Korea