COX1_BLAGE
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 03-AUG-2022, entry version 99.
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; Ectobiidae;
OC Blattellinae; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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
