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Database: UniProt
Entry: G4CJ70_9NEIS
LinkDB: G4CJ70_9NEIS
Original site: G4CJ70_9NEIS 
ID   G4CJ70_9NEIS            Unreviewed;       502 AA.
AC   G4CJ70;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=katA {ECO:0000313|EMBL:EGY52164.1};
GN   ORFNames=HMPREF9371_1659 {ECO:0000313|EMBL:EGY52164.1};
OS   Neisseria shayeganii 871.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=1032488 {ECO:0000313|EMBL:EGY52164.1, ECO:0000313|Proteomes:UP000003019};
RN   [1] {ECO:0000313|EMBL:EGY52164.1, ECO:0000313|Proteomes:UP000003019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=871 {ECO:0000313|EMBL:EGY52164.1,
RC   ECO:0000313|Proteomes:UP000003019};
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 (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
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, ECO:0000256|RuleBase:RU000498}.
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:EGY52164.1}.
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DR   EMBL; AGAY01000059; EGY52164.1; -; Genomic_DNA.
DR   RefSeq; WP_009119349.1; NZ_JH164926.1.
DR   AlphaFoldDB; G4CJ70; -.
DR   STRING; 1032488.HMPREF9371_1659; -.
DR   PATRIC; fig|1032488.3.peg.1569; -.
DR   HOGENOM; CLU_010645_2_0_4; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000003019; 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   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
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:SF61; 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; 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|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
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:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003019}.
FT   DOMAIN          10..394
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         340
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   502 AA;  56735 MW;  D06DBE5BE06D68A8 CRC64;
     MSKCPVTHLT MNNGAPVADN QNSMTAGPRG PLLAQDLWLN EKLANFVREV IPERRMHAKG
     SGAFGTFTVT NDITQYTRAA IFSKVGKKTE MFARFTTVAG ERGAADAERD IRGFALKFYT
     EEGNWDMVGN NTPVFFLRDP RKFPDLNKAV KRDPRTNMRS ATNNWDFWTL LPEAFHQVTI
     VMSDRGIPAT YRHMHGYGSH TYSFWNEAGE RFWVKFHFHT QQGIKNLSNE EAAAIIADDR
     ESHQRDLYES IEKGDFPKWT MYVQIMPEAD AEKVPYHPFD LTKVWPKKDY PLIEVGEFEL
     NRNPENFFAD VEQSAFAPSN LVPGIGVSPD RMLQARLFNY ADAQRYRLGV NHNQIPVNAP
     RCPVHSNARD GYGRVDGNYG STLHYEPNSF GQWQEQAQYA EPPLKINGDA AHWNYREDDA
     DYFSQPRALF NLMSAEQKQV LFNNTAAGMG DAPDFIKYRH IRNCNACDPA YGEGVAKALG
     LTVADAIAAR ESDPALGQPG LL
//
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