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Database: UniProt
Entry: G4CX76_9ACTN
LinkDB: G4CX76_9ACTN
Original site: G4CX76_9ACTN 
ID   G4CX76_9ACTN            Unreviewed;       483 AA.
AC   G4CX76;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Catalase KatA {ECO:0000313|EMBL:EGY77590.1};
DE            EC=1.11.1.6 {ECO:0000313|EMBL:EGY77590.1};
GN   Name=katA {ECO:0000313|EMBL:EGY77590.1};
GN   ORFNames=HMPREF9153_1133 {ECO:0000313|EMBL:EGY77590.1};
OS   Cutibacterium avidum ATCC 25577.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=997355 {ECO:0000313|EMBL:EGY77590.1, ECO:0000313|Proteomes:UP000005332};
RN   [1] {ECO:0000313|EMBL:EGY77590.1, ECO:0000313|Proteomes:UP000005332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25577 {ECO:0000313|EMBL:EGY77590.1,
RC   ECO:0000313|Proteomes:UP000005332};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329}.
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:EGY77590.1}.
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DR   EMBL; AGBA01000013; EGY77590.1; -; Genomic_DNA.
DR   RefSeq; WP_004810220.1; NZ_JH165054.1.
DR   AlphaFoldDB; G4CX76; -.
DR   PATRIC; fig|997355.3.peg.1113; -.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   Proteomes; UP000005332; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
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   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 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|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EGY77590.1};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:EGY77590.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005332}.
FT   DOMAIN          10..392
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         339
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:PIRSR038928-2"
SQ   SEQUENCE   483 AA;  54411 MW;  CE352176FDC53129 CRC64;
     MPIDPSKPST NTNGSPAPSD EYSLTVGADG PVLLHDAHLI DTLAHFNREN IPERKPHAKG
     SGAFGHFETT ADVSEYTKAG FLQKGKETPM LARFSTVAGE LGSPDTWRDV RGFSLKFYTD
     EGNFDMVGNN TPVFFMRDPM KFPHFIRSQK RLPNSGLRSP NMMYDYWSLS PESAHQVAYL
     MGPRGIPLSY RTMNGYSSHT YSWVNAEGKI TWVKYHFISD QGVHTMTADQ AKAVVGDHPD
     LHREDLFNHI ADGDHPSWTV KVQLMPYDDA KDYRFNPFDI TKVWPHKDYP LHTIGRFTLD
     RNPENFFAEI EQAAFSPSNT VEGTGLSPDR MLLSRAFAYN DAARNRLGVN YEQLPVNRPT
     VATNQYTFDG QMTYEHAGSA PTYAPNSYGR DHATGYRAGS EVTWETDGEL VRAAQTLHSE
     DDDFGQAHTL VHDVFSEQER DELVETLVDL LTNFDMEEPV IGNTLTYWRN IDAGIADRVE
     STM
//
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