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Database: UniProt
Entry: C7C6N2_METED
LinkDB: C7C6N2_METED
Original site: C7C6N2_METED 
ID   C7C6N2_METED            Unreviewed;       370 AA.
AC   C7C6N2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   ORFNames=METD_I0111 {ECO:0000313|EMBL:CAX21786.1};
OS   Methylorubrum extorquens (strain DSM 6343 / CIP 106787 / DM4)
OS   (Methylobacterium extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=661410 {ECO:0000313|EMBL:CAX21786.1, ECO:0000313|Proteomes:UP000008070};
RN   [1] {ECO:0000313|Proteomes:UP000008070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6343 / CIP 106787 / DM4
RC   {ECO:0000313|Proteomes:UP000008070};
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
CC   -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000296};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR000296}.
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DR   EMBL; FP103042; CAX21786.1; -; Genomic_DNA.
DR   RefSeq; WP_012778948.1; NC_012988.1.
DR   AlphaFoldDB; C7C6N2; -.
DR   GeneID; 72987502; -.
DR   KEGG; mdi:METDI0111; -.
DR   HOGENOM; CLU_045961_1_0_5; -.
DR   Proteomes; UP000008070; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08153; srpA_like; 1.
DR   Gene3D; 1.20.1280.120; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   PIRSF; PIRSF000296; SrpA; 1.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Iron {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000296,
KW   ECO:0000256|PIRSR:PIRSR000296-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000296,
KW   ECO:0000313|EMBL:CAX21786.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR000296, ECO:0000313|EMBL:CAX21786.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..364
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          347..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         343
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:PIRSR000296-2"
SQ   SEQUENCE   370 AA;  39189 MW;  546EA0FD12D06912 CRC64;
     MTLLHHLTGA PPGMTTRALM LRLAGIGAVL AGTAGAFTYA GGWLSPDALT PARVVDRFEQ
     VNGPHPGFRR NHAKGLCVAG TFASNGAGAR LSKASVFSAG RVTRVEGRVA LAGGQPYAAD
     AAATVRSLAL RFRLPEGEEW RTGMNNIPVF PVRTPEAFYE QLLAAKPDPA TGRPDPERLK
     AFFALHPESA KAAALIKART ITSGFADSTF QSLNTFRFVA SDGRTTPVRW AFVPERRPEP
     GSAAQEAKAD RNVLFDTLAA ELRQEPLHWH LVVTLGQASD ATDDATLPWP SDRESVDVGT
     LTLTGAAPED ADTCRDINFD PLVLPDGIAP SDDPLLSARS AAYARSFTRR AGEEKVPSAV
     AGTSPDGASL
//
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