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Cytochrome c oxidase subunit 1 (EC 1.9.3.1) (Cytochrome c oxidase polypeptide I)

 COX1_NEUCR              Reviewed;         557 AA.
P03945; M1RV30;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 2.
23-MAY-2018, entry version 124.
RecName: Full=Cytochrome c oxidase subunit 1;
EC=1.9.3.1;
AltName: Full=Cytochrome c oxidase polypeptide I;
Name=cox-1; Synonyms=coi, cox1; ORFNames=NCM025, NCU16016;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Mitochondrion.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-99;
234-285; 346-354; 443-489 AND 494-521.
PubMed=6327266;
Burger G., Scriven C., Machleidt W., Werner S.;
"Subunit 1 of cytochrome oxidase from Neurospora crassa: nucleotide
sequence of the coding gene and partial amino acid sequence of the
protein.";
EMBO J. 1:1385-1391(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/BF00365676;
de Jonge J.C., de Vries H.;
"The structure of the gene for subunit I of cytochrome c oxidase in
Neurospora crassa mitochondria.";
Curr. Genet. 7:21-28(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Adiopodoume / FGSC 430;
PubMed=2531370; DOI=10.1093/nar/17.22.9087;
Field D.J., Sommerfield A., Saville B.J., Collins R.A.;
"A group II intron in the Neurospora mitochondrial coI gene:
nucleotide sequence and implications for splicing and molecular
evolution.";
Nucleic Acids Res. 17:9087-9099(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
Kennell J.C., Collins R.A., Griffiths A.J.F., Nargang F.E.;
"Mitochondrial genetics of Neurospora.";
(In) Kueck U. (eds.);
The Mycota II, Genetics and Biotechnology (2nd edition), pp.95-112,
Springer-Verlag, Berlin-Heidelberg (2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 519-557.
PubMed=2949084; DOI=10.1016/0022-2836(86)90447-X;
Burger G., Werner S.;
"Mitochondrial gene URFN of Neurospora crassa codes for a long
polypeptide with highly repetitive structure.";
J. Mol. Biol. 191:589-599(1986).
[7]
MYRISTOYLATION AT LYS-324.
PubMed=7567996; DOI=10.1073/pnas.92.19.8680;
Vassilev A.O., Plesofsky-Vig N., Brambl R.;
"Cytochrome c oxidase in Neurospora crassa contains myristic acid
covalently linked to subunit 1.";
Proc. Natl. Acad. Sci. U.S.A. 92:8680-8684(1995).
-!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
chain that catalyzes the reduction of oxygen to water. Subunits 1-
3 form the functional core of the enzyme complex. CO I is the
catalytic subunit of the enzyme. Electrons originating in
cytochrome c are transferred via the copper A center of subunit 2
and heme A of subunit 1 to the bimetallic center formed by heme A3
and copper B.
-!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
ferricytochrome c + 2 H(2)O.
-!- PATHWAY: Energy metabolism; oxidative phosphorylation.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
membrane protein.
-!- PTM: The amino end of the mature protein may be Ser-3.
-!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X01850; CAA25976.1; -; Genomic_DNA.
EMBL; M36958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X14669; CAA32799.1; -; Genomic_DNA.
EMBL; KC683708; AGG16005.1; -; Genomic_DNA.
EMBL; X04512; CAA28195.1; -; Genomic_DNA.
PIR; A00469; ODNC1.
RefSeq; YP_009126717.1; NC_026614.1.
ProteinModelPortal; P03945; -.
iPTMnet; P03945; -.
EnsemblFungi; AGG16005; AGG16005; NCU16016.
GeneID; 23681570; -.
KEGG; ncr:NCU16016; -.
EuPathDB; FungiDB:NCU16016; -.
InParanoid; P03945; -.
KO; K02256; -.
OrthoDB; EOG092C2KU4; -.
UniPathway; UPA00705; -.
Proteomes; UP000001805; Mitochondrion.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
CDD; cd01663; Cyt_c_Oxidase_I; 1.
Gene3D; 1.20.210.10; -; 1.
InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
InterPro; IPR000883; Cyt_C_Oxase_1.
InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
InterPro; IPR033944; Cyt_c_oxase_su1_dom.
PANTHER; PTHR10422; PTHR10422; 1.
Pfam; PF00115; COX1; 1.
PRINTS; PR01165; CYCOXIDASEI.
SUPFAM; SSF81442; SSF81442; 1.
PROSITE; PS50855; COX1; 1.
PROSITE; PS00077; COX1_CUB; 1.
1: Evidence at protein level;
Complete proteome; Copper; Direct protein sequencing;
Electron transport; Heme; Iron; Lipoprotein; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane; Myristate;
Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 557 Cytochrome c oxidase subunit 1.
/FTId=PRO_0000183366.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TRANSMEM 69 89 Helical. {ECO:0000255}.
TRANSMEM 106 126 Helical. {ECO:0000255}.
TRANSMEM 151 171 Helical. {ECO:0000255}.
TRANSMEM 187 207 Helical. {ECO:0000255}.
TRANSMEM 240 260 Helical. {ECO:0000255}.
TRANSMEM 272 292 Helical. {ECO:0000255}.
TRANSMEM 310 330 Helical. {ECO:0000255}.
TRANSMEM 343 363 Helical. {ECO:0000255}.
TRANSMEM 378 398 Helical. {ECO:0000255}.
TRANSMEM 418 438 Helical. {ECO:0000255}.
TRANSMEM 457 477 Helical. {ECO:0000255}.
METAL 67 67 Iron (heme A axial ligand).
{ECO:0000305}.
METAL 246 246 Copper B. {ECO:0000305}.
METAL 250 250 Copper B. {ECO:0000305}.
METAL 295 295 Copper B. {ECO:0000305}.
METAL 296 296 Copper B. {ECO:0000305}.
METAL 381 381 Iron (heme A3 axial ligand).
{ECO:0000305}.
METAL 383 383 Iron (heme A axial ligand).
{ECO:0000305}.
LIPID 324 324 N6-myristoyl lysine.
{ECO:0000269|PubMed:7567996}.
CROSSLNK 246 250 1'-histidyl-3'-tyrosine (His-Tyr).
{ECO:0000250}.
CONFLICT 527 527 V -> A (in Ref. 1; CAA25976 and 3;
CAA28195). {ECO:0000305}.
SEQUENCE 557 AA; 61522 MW; 8AC9618704E5C91D CRC64;
MSSISIWTER WFLSTNAKDI GVLYLIFALF SGLLGTAFSV LIRMELSGPG VQYIADNQLY
NAIITAHAIL MIFFMVMPAL IGGFGNFLLP LLVGGPDMAF PRLNNISFWL LPPSLLLLVF
SACIEGGAGT GWTIYPPLSG VQSHSGPSVD LAIFALHLSG VSSLLGSINF ITTIVNMRTP
GIRLHKLALF GWAVVITAVL LLLSLPVLAG AITMLLTDRN FNTSFFETAG GGDPILFQHL
FWFFGHPEVY ILIIPGFGII STTISAYSNK SVFGYIGMVY AMMSIGILGF IVWSHHMYTV
GLDVDTRAYF TAATLIIAVP TGIKIFSWLA TCYGGSIRLT PSMLFALGFV FMFTIGGLSG
VVLANASLDI AFHDTYYVVA HFHYVLSMGA VFAMFSGWYH WVPKILGLNY NMVLSKAQFW
LLFIGVNLTF FPQHFLGLQG MPRRISDYPD AFSGWNLISS FGSIVSVVAS WLFLYIVYIQ
LVQGEYAGRY PWSIPQFYTD SLRALLNRSY PSLEWSISSP PKPHSFVSLP LQSSSFFLSF
FRLSSYGEQK EISGRQN


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