ID C3Y7C5_BRAFL Unreviewed; 452 AA.
AC C3Y7C5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_82809 {ECO:0000313|EMBL:EEN63753.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN63753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN63753.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN63753.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00001937};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
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DR EMBL; GG666489; EEN63753.1; -; Genomic_DNA.
DR RefSeq; XP_002607743.1; XM_002607697.1.
DR AlphaFoldDB; C3Y7C5; -.
DR STRING; 7739.C3Y7C5; -.
DR eggNOG; KOG0047; Eukaryota.
DR InParanoid; C3Y7C5; -.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 2.40.180.10; Catalase core domain; 2.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; CATALASE; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT DOMAIN 1..139
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN63753.1"
SQ SEQUENCE 452 AA; 51428 MW; 79386E40800D1E3E CRC64;
PSWTLKIQVM TFEEAEKFRF NPFDLTKVWP QGEFPLIPVG KMVLNRNPKN YFAEVEQIAF
SPIHMVPGIE ASPDKMLQGR LFSYSDTHRH RLGSNYLQIP VNCPYRARVT NYQRDGPQCV
DDNQAGAPNC YPNSFSGPKQ KETIIQRHLV EPGAPNYYPN SFSGPEQNET ITPPAIKTTG
DLQRYNTADE DNFTQVGTFW RNVLSEYDRE HLVDNLASHM TAAQEFLQKR AVKNFSQCDP
EYGRRLQEKL DKYNAAKTIQ LQFVSKQERQ ILNKNPTYRG TLIQEYRKDG DPKIKVFRAE
NSESVNKENA ILTVYSYRSI PPGGGTYVVL QFKASKMYFT AKKTKPGKLI LQEPGEFDPE
DAEDITTTAD RRVFLVKPSQ PGSSDVVFAS QHKSGDNKNK ARVITLLKNR GVPAKFKREG
KGPLESQWFQ IEHVLAGGAS EQRDEGQVQG VY
//
