ID A0A2W1JQJ1_9CYAN Unreviewed; 764 AA.
AC A0A2W1JQJ1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Catalase-peroxidase {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE Short=CP {ECO:0000256|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000256|HAMAP-Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
DE AltName: Full=Peroxidase/catalase {ECO:0000256|HAMAP-Rule:MF_01961};
GN Name=katG_2 {ECO:0000313|EMBL:PZD73152.1};
GN Synonyms=katG {ECO:0000256|HAMAP-Rule:MF_01961};
GN ORFNames=C1752_02402 {ECO:0000313|EMBL:PZD73152.1};
OS Acaryochloris thomasi RCC1774.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris; Acaryochloris thomasi.
OX NCBI_TaxID=1764569 {ECO:0000313|EMBL:PZD73152.1, ECO:0000313|Proteomes:UP000248857};
RN [1] {ECO:0000313|EMBL:PZD73152.1, ECO:0000313|Proteomes:UP000248857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC1774 {ECO:0000313|EMBL:PZD73152.1,
RC ECO:0000313|Proteomes:UP000248857};
RX PubMed=29904088; DOI=10.1038/s41598-018-27542-7;
RA Partensky F., Six C., Ratin M., Garczarek L., Vaulot D., Probert I.,
RA Calteau A., Gourvil P., Marie D., Grebert T., Bouchier C., Le Panse S.,
RA Gachenot M., Rodriguez F., Garrido J.L.;
RT "A novel species of the marine cyanobacterium Acaryochloris with a unique
RT pigment content and lifestyle.";
RL Sci. Rep. 8:9142-9142(2018).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000256|HAMAP-Rule:MF_01961}.
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=1.11.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001378, ECO:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01961, ECO:0000256|RuleBase:RU003451};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000256|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_01961}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000256|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01961,
CC ECO:0000256|RuleBase:RU003451}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01961}.
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:PZD73152.1}.
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DR EMBL; PQWO01000006; PZD73152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1JQJ1; -.
DR OrthoDB; 9759743at2; -.
DR Proteomes; UP000248857; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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 CDD; cd08200; catalase_peroxidase_2; 1.
DR Gene3D; 1.10.520.10; -; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2.
DR HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR NCBIfam; TIGR00198; cat_per_HPI; 1.
DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01961};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01961};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01961};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_01961}; Reference proteome {ECO:0000313|Proteomes:UP000248857}.
FT DOMAIN 152..449
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT BINDING 291
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT SITE 97
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
FT CROSSLNK 250..276
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-
FT 100)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01961"
SQ SEQUENCE 764 AA; 84987 MW; CACB057488A7D271 CRC64;
MNNTPTAAPA QCPFRGTRVG GALGSKPQTD DWWPNRLQVE LLHTQSSQAN PLRDFNYQEA
FEKIDFEQLK SDIKALLTDS KDWWPADYGN YGPQMVRMAW HAAGTYRIAD GRGGAGQGMQ
RFAPLNSWWD NGNTDKSRRL LWPIKQQYGA ALSWADLMAL TGNCALEIMG FKTFGFGGGR
IDAWEADRST YWGSEFWNGQ SLEESGERGK QHAGHPDQMV TREIRWVGKP DEEHYDLENP
LAASHQALIY VDPEGPNGEG DPAASARDIR ETFARMGMND EETVALIAGG HAFGKSHGMV
EPDKIGPAPE AAPLQAMGLG WQNPKGTGFA QYTMTNGIEG SWTPDPTQWD NSYLENLFKY
DWEKTESPAG SIQWQPSSPD APKTPDAHQP NVEHSLMMMT SDLALKVDPA YHEICQRFVG
DFDDFSDAFA RAWYKLMHRD MGPKARYLGP EVAKEDLPWQ DPIPALDHDV VGDADIDALK
HKILESGLSV SALVSAAWAS ASTYRDTDKR GGANGARVGL DPQKDWEMNR PQELGEVLSA
LEQIQSDFNG AQSGSKKISM ADLIVLGGCA AVEKAAQDAG VSVSVPFTPG RMDTTQEMTD
VESFNWLKPV SDGFRNYHND AIGFKVKPER IFLDRAHLLT LTAPEWTALV GGLRALDQNW
DHSKHGVFTD RPGVLTNDFF RVLTSMDYEW KPADDRERLF EICDRKSGET KFTATSCDLI
FGSNAELRQV AEVYGADDGH ERMVKDFVAA WDKVMMLDRF DVHA
//