CCON1_PSEST
ID CCON1_PSEST Reviewed; 474 AA.
AC D9IA43;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit CcoN1 {ECO:0000303|PubMed:20576851, ECO:0000312|EMBL:ADI99999.1};
DE EC=7.1.1.9 {ECO:0000305};
DE AltName: Full=Cytochrome CBB3 subunit CcoN1 {ECO:0000250|UniProtKB:Q05572, ECO:0000312|PDB:3MK7};
GN Name=ccoN1 {ECO:0000312|EMBL:ADI99999.1};
OS Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=316;
RN [1] {ECO:0000312|EMBL:ADI99999.1, ECO:0000312|PDB:3MK7}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12; 25-34; 60-66;
RP 225-238; 262-271; 302-309; 335-352; 410-449 AND 457-474, X-RAY
RP CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-474 IN COMPLEX WITH HEME AND COPPER,
RP COFACTOR, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC 568 / 218 / ZoBell 632 {ECO:0000312|EMBL:ADI99999.1};
RX PubMed=20576851; DOI=10.1126/science.1187303;
RA Buschmann S., Warkentin E., Xie H., Langer J.D., Ermler U., Michel H.;
RT "The structure of cbb3 cytochrome oxidase provides insights into proton
RT pumping.";
RL Science 329:327-330(2010).
CC -!- FUNCTION: Cbb3-type cytochrome c oxidase is the component of the
CC respiratory chain that catalyzes the reduction of oxygen to water.
CC Subunits CcoN and CcoO form the functional core of the enzyme complex.
CC Subunits CcoP and CcoQ may optionally bind to the core. CcoN is the
CC catalytic subunit of the enzyme. Electrons originating in cytochrome c
CC or a quinol are transferred to the bimetallic center formed by a high-
CC spin heme and copper B. The complex also functions as a proton pump.
CC {ECO:0000305}.
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; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:20576851};
CC Note=Binds 1 copper ion per subunit, denoted as copper B.
CC {ECO:0000269|PubMed:20576851};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:20576851};
CC Note=Binds 2 heme b groups per subunit, denoted as high- and low-spin.
CC {ECO:0000269|PubMed:20576851};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000305}.
CC -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase at least
CC composed of CcoN, CcoO, CcoQ and CcoP. {ECO:0000269|PubMed:20576851}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0ABI8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000255|RuleBase:RU000370}.
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DR EMBL; HM130676; ADI99999.1; -; Genomic_DNA.
DR RefSeq; WP_003285488.1; NZ_CP036186.1.
DR PDB; 3MK7; X-ray; 3.20 A; A/D/G/K=1-474.
DR PDB; 5DJQ; X-ray; 3.20 A; A/D/G/K=1-474.
DR PDBsum; 3MK7; -.
DR PDBsum; 5DJQ; -.
DR AlphaFoldDB; D9IA43; -.
DR SMR; D9IA43; -.
DR STRING; 32042.PstZobell_19483; -.
DR eggNOG; COG3278; Bacteria.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; D9IA43; -.
DR GO; GO:0070069; C:cytochrome complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070470; C:plasma membrane respirasome; IC:UniProtKB.
DR GO; GO:0045278; C:plasma membrane respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IC:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IC:UniProtKB.
DR GO; GO:0019825; F:oxygen binding; IC:UniProtKB.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IC:UniProtKB.
DR GO; GO:0019646; P:aerobic electron transport chain; IC:UniProtKB.
DR GO; GO:0019411; P:aerobic respiration, using ferrous ions as electron donor; IC:UniProtKB.
DR GO; GO:0015990; P:electron transport coupled proton transport; IC:UniProtKB.
DR GO; GO:0006119; P:oxidative phosphorylation; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
DR CDD; cd01661; cbb3_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; IPR004677; Cyt_c_oxidase_cbb3_su1.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR PANTHER; PTHR10422:SF29; PTHR10422:SF29; 1.
DR Pfam; PF00115; COX1; 1.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR00780; ccoN; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Copper;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..474
FT /note="Cbb3-type cytochrome c oxidase subunit CcoN1"
FT /id="PRO_0000433597"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..60
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..129
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 151..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..205
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..270
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..345
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..432
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 60
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20576851,
FT ECO:0007744|PDB:3MK7"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:20576851,
FT ECO:0007744|PDB:3MK7"
FT BINDING 257
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:20576851,
FT ECO:0007744|PDB:3MK7"
FT BINDING 258
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000269|PubMed:20576851,
FT ECO:0007744|PDB:3MK7"
FT BINDING 345
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2; high-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20576851,
FT ECO:0007744|PDB:3MK7"
FT BINDING 347
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1; low-spin"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:20576851,
FT ECO:0007744|PDB:3MK7"
FT HELIX 12..40
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3MK7"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:3MK7"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 128..150
FT /evidence="ECO:0007829|PDB:3MK7"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 159..178
FT /evidence="ECO:0007829|PDB:3MK7"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3MK7"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 195..212
FT /evidence="ECO:0007829|PDB:3MK7"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:3MK7"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 305..327
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 354..369
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 379..411
FT /evidence="ECO:0007829|PDB:3MK7"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 423..429
FT /evidence="ECO:0007829|PDB:3MK7"
FT HELIX 431..460
FT /evidence="ECO:0007829|PDB:3MK7"
SQ SEQUENCE 474 AA; 52789 MW; 5EC7997C47C7295C CRC64;
MNTATSTAYS YKVVRQFAIM TVVWGIVGMG LGVFIAAQLA WPFLNFDLPW TSFGRLRPLH
TNAVIFAFGG CALFATSYYS VQRTCQTTLF APKLAAFTFW GWQLVILLAA ISLPLGFTSS
KEYAELEWPI DILITIVWVA YAVVFFGTLA KRKVKHIYVG NWFFGAFILT VAILHVVNNL
EIPVTAMKSY SLYAGATDAM VQWWYGHNAV GFFLTAGFLG IMYYFVPKQA ERPVYSYRLS
IVHFWALITV YIWAGPHHLH YTALPDWAQS LGMVMSLILL APSWGGMING MMTLSGAWHK
LRSDPILRFL VVSLAFYGMS TFEGPMMAIK TVNALSHYTD WTIGHVHAGA LGWVAMVSIG
ALYHLVPKVF GREQMHSIGL INTHFWLATI GTVLYIASMW VNGIAQGLMW RAINDDGTLT
YSFVESLEAS HPGFVVRMIG GAIFFAGMLV MAYNTWRTVQ AAKPAEYDAA AQIA
