ID   M9YGN9_AZOVI            Unreviewed;       464 AA.
AC   M9YGN9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Di-heme cytochrome c peroxidase, CCP MauG family {ECO:0000313|EMBL:AGK19674.1};
GN   ORFNames=AvCA6_10230 {ECO:0000313|EMBL:AGK19674.1};
OS   Azotobacter vinelandii CA6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK19674.1, ECO:0000313|Proteomes:UP000012988};
RN   [1] {ECO:0000313|EMBL:AGK19674.1, ECO:0000313|Proteomes:UP000012988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CA6 {ECO:0000313|EMBL:AGK19674.1,
RC   ECO:0000313|Proteomes:UP000012988};
RX   PubMed=23792740; DOI=10.1128/genomeA.00313-13;
RA   Noar J.D., Bruno-Barcena J.M.;
RT   "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain CA
RT   and Tungsten-Tolerant Mutant Strain CA6.";
RL   Genome Announc. 1:E00313-E00313(2013).
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DR   EMBL; CP005095; AGK19674.1; -; Genomic_DNA.
DR   RefSeq; WP_012699678.1; NC_021150.1.
DR   AlphaFoldDB; M9YGN9; -.
DR   KEGG; avd:AvCA6_10230; -.
DR   PATRIC; fig|1283331.3.peg.970; -.
DR   HOGENOM; CLU_034652_2_0_6; -.
DR   Proteomes; UP000012988; Chromosome.
DR   GO; GO:0009055; F:electron transfer 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:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   InterPro; IPR025992; Haem-bd.
DR   PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   PANTHER; PTHR30600:SF7; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   Pfam; PF14376; Haem_bd; 1.
DR   SMART; SM01235; Haem_bd; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:AGK19674.1};
KW   Peroxidase {ECO:0000313|EMBL:AGK19674.1}.
FT   DOMAIN          184..316
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          336..455
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   464 AA;  50983 MW;  13DDFD513371E277 CRC64;
     MKKLPLVIGA CVAGYLATVF IVDRFDVRLS EQHLASAQLN GMDKLTSEAF KVLNSNGCQY
     CHTRNSELPF YANMPIAKQL MNKDIELAQR QFNIESLLAS AQQGKAVSEV DLAKIESVMQ
     DNAMPPNLYL GMHWRSRLSD EEKGVLLDWV KAERLKQSSA DAVADAYKYE PVQPITTSFP
     VNPAKVALGE KLYHDTRLSS DDTVSCASCH ALDKGGVDRL DVSVGVGGSK GPINAPTVYN
     AAFNVLQFWD GRAADLQKQA GGPPMNPLEM ASTSWEQIVG KLTQDAQLSA EFAALYPEGI
     TENSITDAIA EFEKTLVTPN SRFDLFLKGQ GDALSSVEKE GYELFKTAKC ATCHVGEAMG
     GQSFELMGIK KDYFADRGNV SEVDHGRYNV TKDPHDMYRF KVPTLRNVAL TAPYFHDASA
     KTLEDAVDKM AEYQVGMKLS KDEIGKIVAF LQTLNGEYQG KTLQ
//