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Database: UniProt
Entry: A0A2W1JQJ1_9CYAN
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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
//
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