ID A0A1Q7A3X0_9CHLR Unreviewed; 358 AA.
AC A0A1Q7A3X0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE SubName: Full=Catalase {ECO:0000313|EMBL:OLB56804.1};
DE Flags: Fragment;
GN ORFNames=AUI01_05850 {ECO:0000313|EMBL:OLB56804.1};
OS Ktedonobacter sp. 13_2_20CM_2_56_8.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805232 {ECO:0000313|EMBL:OLB56804.1, ECO:0000313|Proteomes:UP000186629};
RN [1] {ECO:0000313|EMBL:OLB56804.1, ECO:0000313|Proteomes:UP000186629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLB56804.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNDS01000097; OLB56804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7A3X0; -.
DR Proteomes; UP000186629; Unassembled WGS sequence.
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; 1.
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..252
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OLB56804.1"
SQ SEQUENCE 358 AA; 41531 MW; 309700CF52FD0E0E CRC64;
KFQDFIHSQK RMPDTDLRSN NAQWDFWSLS PESAHQVTFL MSDRGTPRTW RNMNGYSSHT
YMWINAKGER VWVKYHFKTE QGIQNFTDAE AKAMTAEDPD YHRRDLRQAI QRKEYPVWRL
EMQIMPFEDA ASYRFNPFDL TKVWPHKDYP PITIGRMVLD RNPENFFTEI EQAAFEPSNM
VSGIGPSPDK MLLGRLFSYA DTHRYRIGTN YKQLPVNAPQ VEVHSYNKDG AMRYRHNGTQ
PVYAPNSYGG PQADPQRYPE PSWFASGEIM RSAYTPHAED NDFVQPGNLY RHVMSETDRE
HLVTNIVGHM SQGVERFIQE RTVTTYWYQV DPDLGTRVAE GLGLKIATEL PTSVGGGE
//
