ID A0A0J8VK44_9ENTR Unreviewed; 752 AA.
AC A0A0J8VK44;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN Name=katE {ECO:0000313|EMBL:KMV33833.1};
GN ORFNames=ACH50_14065 {ECO:0000313|EMBL:KMV33833.1};
OS Franconibacter pulveris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Franconibacter.
OX NCBI_TaxID=435910 {ECO:0000313|EMBL:KMV33833.1, ECO:0000313|Proteomes:UP000037315};
RN [1] {ECO:0000313|EMBL:KMV33833.1, ECO:0000313|Proteomes:UP000037315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ34 {ECO:0000313|EMBL:KMV33833.1,
RC ECO:0000313|Proteomes:UP000037315};
RA Pal S., Banerjee T.D., Roy A., Sar P., Kazy S.K.;
RT "Genome sequencing of Cronobacter sp. strain DJ34 isolated from petroleum
RT contaminated sludge of Duliajan Oil Fields, Assam, India.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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:KMV33833.1}.
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DR EMBL; LFEJ01000018; KMV33833.1; -; Genomic_DNA.
DR RefSeq; WP_024559613.1; NZ_LFEJ01000018.1.
DR AlphaFoldDB; A0A0J8VK44; -.
DR STRING; 1121863.GCA_000621185_02949; -.
DR PATRIC; fig|1656095.3.peg.703; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000037315; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08155; catalase_clade_2; 1.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927}.
FT DOMAIN 80..468
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 200
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 124
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 164
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 213
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 410
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 414
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-2"
FT BINDING 421
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 752 AA; 84217 MW; 03A0C6D232DD63B9 CRC64;
MSQEEKKPHH HESPVHDADE SRPGLDSLAP EDGSHRPDPV PTPPGEQPTA PGSLKAPDTS
NEKLKALETF RKGSEDFPLT TNQGVRIADD QNSLRAGTRG PTLLEDFILR EKITHFDHER
IPERIVHARG SAAHGYFQPY KSLSHITKAD FLSDPDKITP VFVRFSTVQG GAGSADTVRD
IRGFATKFYT QEGIFDLVGN NTPVFFIQDA HKFPDFVHAV KPEPHWAIPQ GQSAHDTFWD
YVSLQPETLH NVIWAMSDRG IPRSYRTMEG FGIHTFRMIN AEGKATFVRF HWKPVAGKAS
LLWDESQKLT GRDPDFHRRD LWEAIEAGDF PEYELGLQLI PEEDEFKFDF DLLDATKLIP
EELVPVQLVG KMVLNRNPDN FFAENEQAAF HPGHIVPGLD FTNDPLLQGR LFSYTDTQIS
RLGGPNFHEI PINRPTCPYH NFQRDGMHRM DIDTNPANYE PNSINDNWPR ETPPGPKRGG
FESYQERIEG YKVRERSPSF GEYYAHPRLF WQSQTPVEQR HIIDAFSFEL SKVVRPYIRE
RVVDQLCRID ISLAQPVAEN LGIELTDEQM HIAPPKDVNG LKKDASLSLY AVPGGSVKGR
VVAVLLNDKV NGAELLSVLQ KLKTHGVHAK LLYKRMGEAV ADDGSRIPVA GTFAGSPSLT
VDAVIVPGGD VASILDNADA AYYLMEAYKH LKVIALLGEA RQFKPFIKVP DAGEEGVLEA
DDATGNFTDD FVKLLAGHRI WSRTTKSLTI PA
//
