ID O66533_AQUAE Unreviewed; 355 AA.
AC O66533;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:AAC06485.1};
GN Name=cpx {ECO:0000313|EMBL:AAC06485.1};
GN OrderedLocusNames=aq_136 {ECO:0000313|EMBL:AAC06485.1};
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324 {ECO:0000313|EMBL:AAC06485.1, ECO:0000313|Proteomes:UP000000798};
RN [1] {ECO:0000313|EMBL:AAC06485.1, ECO:0000313|Proteomes:UP000000798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5 {ECO:0000313|EMBL:AAC06485.1,
RC ECO:0000313|Proteomes:UP000000798};
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olson G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC 1}.
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DR EMBL; AE000657; AAC06485.1; -; Genomic_DNA.
DR PIR; B70313; B70313.
DR RefSeq; NP_213093.1; NC_000918.1.
DR RefSeq; WP_010880031.1; NC_000918.1.
DR AlphaFoldDB; O66533; -.
DR STRING; 224324.aq_136; -.
DR PeroxiBase; 5036; AaeoDiHCcP.
DR EnsemblBacteria; AAC06485; AAC06485; aq_136.
DR KEGG; aae:aq_136; -.
DR PATRIC; fig|224324.8.peg.116; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_1_1_0; -.
DR InParanoid; O66533; -.
DR OrthoDB; 9772811at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IBA:GO_Central.
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 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; IPR026259; MauG/Cytc_peroxidase.
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 PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000294-2};
KW Oxidoreductase {ECO:0000313|EMBL:AAC06485.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:AAC06485.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000798};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 51..182
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 204..330
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 73
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 76
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 77
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT BINDING 93
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT BINDING 218
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 221
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 222
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT BINDING 305
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
SQ SEQUENCE 355 AA; 39876 MW; 93F76BF23A4C4905 CRC64;
MRKGLLLMAV FAGFVVAKEK IDDKELLKMA RQYFKPLPKV AENPQNPVTP EKVKLGKMLY
YDPRLSKSGL ISCNTCHNLA RYGVDNLPTS IGHRWAIGPR NAPTVYNAAI HIAQFWDGRA
KDVEEQALGP IVNPIEMANT EENAVKTLKS IPEYVELFKK AFPNEKDPVK YENIGKAIGA
FERTLMTPSR FDEFLKGNTK ALTEQEKRGL KTFIEVGCVA CHNGPGVGGN MFAKFGMITE
YWKVTYPYVL VGKPAIKVDF GRFGVTKKEE DMFVFKVPSL RNIEHTYPYF HDGSVWSLED
AVRIMAKTQL GKELTDQQVK DIVAFLKALT GKIPKHALEV PELPPSTDKT PKPEL
//
