ID   COX1_BLAGE              Reviewed;         508 AA.
AC   Q36724;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 102.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
DE   Flags: Fragment;
GN   Name=COI;
OS   Blattella germanica (German cockroach) (Blatta germanica).
OG   Mitochondrion {ECO:0000312|EMBL:AAB31450.2}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blattellidae;
OC   Blattella.
OX   NCBI_TaxID=6973 {ECO:0000312|EMBL:AAB31450.2};
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAB31450.2}
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=8044176; DOI=10.1016/0965-1748(94)90098-1;
RA   Martinez-Gonzalez J., Hegardt F.G.;
RT   "Cytochrome c oxidase subunit I from the cockroach Blattella germanica:
RT   cloning, developmental pattern and tissue expression.";
RL   Insect Biochem. Mol. Biol. 24:619-626(1994).
CC   -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC       mitochondrial electron transport chain which drives oxidative
CC       phosphorylation. The respiratory chain contains 3 multisubunit
CC       complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC       cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC       CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC       transfer electrons derived from NADH and succinate to molecular oxygen,
CC       creating an electrochemical gradient over the inner membrane that
CC       drives transmembrane transport and the ATP synthase. Cytochrome c
CC       oxidase is the component of the respiratory chain that catalyzes the
CC       reduction of oxygen to water. Electrons originating from reduced
CC       cytochrome c in the intermembrane space (IMS) are transferred via the
CC       dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC       to the active site in subunit 1, a binuclear center (BNC) formed by
CC       heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC       water molecules using 4 electrons from cytochrome c in the IMS and 4
CC       protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds 2 heme A groups non-covalently per subunit.
CC       {ECO:0000250|UniProtKB:P00401};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P00401};
CC       Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P00401}.
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of a catalytic core of 3 subunits and
CC       several supernumerary subunits. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC       complex, complex III, CIII). {ECO:0000250|UniProtKB:P00401}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P00401}.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels
CC       in gut and fat body, lower levels in ovary and collateral glands.
CC       {ECO:0000269|PubMed:8044176}.
CC   -!- DEVELOPMENTAL STAGE: Levels increase 3-fold during embryo development
CC       with the highest level in 17 day old embryos. Relatively low levels in
CC       larvae and adults. {ECO:0000269|PubMed:8044176}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; S72627; AAB31450.2; -; mRNA.
DR   AlphaFoldDB; Q36724; -.
DR   SMR; Q36724; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; NAS:UniProtKB.
DR   GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; NAS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR   Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR   InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR   InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR   InterPro; IPR000883; Cyt_C_Oxase_1.
DR   InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR   InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           <1..508
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183295"
FT   TOPO_DOM        <1..6
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        7..35
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        36..45
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        46..81
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        82..89
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        90..112
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        113..135
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        136..165
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        166..177
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        178..207
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        208..222
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        223..256
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        257..264
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        265..281
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        282..293
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        294..322
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        323..330
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        331..352
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        353..365
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        366..395
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        396..401
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        402..428
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        429..441
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        442..473
FT                   /note="Helical; Name=XII"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        474..508
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         40
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         56
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         235
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         239
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         285
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         286
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         363
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         364
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with subunit 2"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         371
FT                   /ligand="heme a3"
FT                   /ligand_id="ChEBI:CHEBI:83282"
FT                   /ligand_note="high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   BINDING         373
FT                   /ligand="Fe(II)-heme a"
FT                   /ligand_id="ChEBI:CHEBI:61715"
FT                   /ligand_note="low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   CROSSLNK        235..239
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P00401"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AAB31450.2"
SQ   SEQUENCE   508 AA;  56001 MW;  48B5BE46771C10DD CRC64;
     WLFSTNHKDI GTLYFIFGAW SGMVGMSLSM LIRAELNQPG SLIGDDQIYN VIVTAHAFVM
     IFFMVMPILI GGFGNWLVPL MLGAPDMAFP RMNNMSFWFL PPSLSLLLAS SLVESGAGTG
     WTLYPPLASG IAHAGASVDL AIFSLHLAGV SSILGAVNFI STIINMKPIN MSPERIPLFV
     WSVGITALLL LLSLPVLAGA ITMLLTDRNL NTSFFDPAGG GDPILYQHLF WFFGHPEVYI
     LILPGFGMIS HIICHESGKK EAFGNLGMIF AMLAIGLLGF VVWAHHMFTV GMDVDTRAYF
     TSATMIIAVP TGIKIFSWLA TMYGSQLTYS APCLWALGFV FLFTVGGLTG VVLANSSIDI
     VLHDTYYVVA HFHYVLSMGA VFAIMAGFIQ WYPLFTGLSL NPKWLKIQFS IMFLGVNLTF
     FPQHFLGLAG MPRRYSDYPD AYTAWNVISS IGSMISFVAV LMFIFIMWES MSSNRQVLFP
     TQTSNSIEWF QNIPPAEHSY AELPTISY
//