COX1B_PARDE
ID COX1B_PARDE Reviewed; 558 AA.
AC P98002;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cytochrome c oxidase subunit 1-beta;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 1-beta;
DE AltName: Full=Cytochrome c oxidase polypeptide I-beta;
GN Name=ctaDII;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Pd 1222;
RX PubMed=2155830; DOI=10.1016/0014-5793(90)80609-m;
RA Raitio M., Pispa J.M., Metso T., Saraste M.;
RT "Are there isoenzymes of cytochrome c oxidase in Paracoccus
RT denitrificans?";
RL FEBS Lett. 261:431-435(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7651515; DOI=10.1038/376660a0;
RA Iwata S., Ostermeier C., Ludwig B., Michel H.;
RT "Structure at 2.8-A resolution of cytochrome c oxidase from Paracoccus
RT denitrificans.";
RL Nature 376:660-669(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=9380672; DOI=10.1073/pnas.94.20.10547;
RA Ostermeier C., Harrenga A., Ermler U., Michel H.;
RT "Structure at 2.7-A resolution of the Paracoccus denitrificans two-subunit
RT cytochrome c oxidase complexed with an antibody FV fragment.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10547-10553(1997).
RN [4]
RP COVALENT BOND.
RX PubMed=10338009; DOI=10.1110/ps.8.5.985;
RA Buse G., Soulimane T., Dewor M., Meyer H.E., Blueggel M.;
RT "Evidence for a copper-coordinated histidine-tyrosine cross-link in the
RT active site of cytochrome oxidase.";
RL Protein Sci. 8:985-990(1999).
RN [5]
RP REVIEW.
RX PubMed=8794157; DOI=10.1016/s0959-440x(96)80110-2;
RA Ostermeier C., Iwata S., Michel H.;
RT "Cytochrome c oxidase.";
RL Curr. Opin. Struct. Biol. 6:460-466(1996).
CC -!- FUNCTION: Subunit I and II form the functional core of the enzyme
CC complex. Electrons originating in cytochrome c are transferred via heme
CC a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This
CC cytochrome c oxidase shows proton pump activity across the membrane in
CC addition to the electron transfer.
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 -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 copper B ion per subunit.;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 2 heme groups per subunit.;
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- PTM: His-276 and Tyr-280 are involved in the formation of a copper-
CC coordinated covalent cross-link at the active site of the catalytic
CC subunit I.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; Y07533; CAA68821.1; -; Genomic_DNA.
DR PIR; S08270; S08270.
DR RefSeq; WP_011748228.1; NZ_PPGA01000019.1.
DR PDB; 1AR1; X-ray; 2.70 A; A=1-558.
DR PDB; 1QLE; X-ray; 3.00 A; A=17-554.
DR PDB; 3EHB; X-ray; 2.32 A; A=1-558.
DR PDB; 3HB3; X-ray; 2.25 A; A=1-558.
DR PDB; 7ATE; EM; 2.40 A; A=1-558.
DR PDB; 7ATN; EM; 2.66 A; A=1-558.
DR PDB; 7AU3; EM; 2.56 A; A=1-558.
DR PDB; 7AU6; EM; 2.40 A; A=1-558.
DR PDBsum; 1AR1; -.
DR PDBsum; 1QLE; -.
DR PDBsum; 3EHB; -.
DR PDBsum; 3HB3; -.
DR PDBsum; 7ATE; -.
DR PDBsum; 7ATN; -.
DR PDBsum; 7AU3; -.
DR PDBsum; 7AU6; -.
DR AlphaFoldDB; P98002; -.
DR SMR; P98002; -.
DR DIP; DIP-6088N; -.
DR IntAct; P98002; 1.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR TCDB; 3.D.4.6.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR OMA; PVDFQYH; -.
DR BRENDA; 7.1.1.9; 3341.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P98002; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
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 InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 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; Disulfide bond;
KW Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron;
KW Membrane; Metal-binding; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..558
FT /note="Cytochrome c oxidase subunit 1-beta"
FT /id="PRO_0000183456"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT TRANSMEM 29..59
FT /note="Helical; Name=I"
FT TOPO_DOM 60..82
FT /note="Periplasmic"
FT TRANSMEM 83..120
FT /note="Helical; Name=II"
FT TOPO_DOM 121..126
FT /note="Cytoplasmic"
FT TRANSMEM 127..151
FT /note="Helical; Name=III"
FT TOPO_DOM 152..176
FT /note="Periplasmic"
FT TRANSMEM 177..206
FT /note="Helical; Name=IV"
FT TOPO_DOM 207..217
FT /note="Cytoplasmic"
FT TRANSMEM 218..251
FT /note="Helical; Name=V"
FT TOPO_DOM 252..262
FT /note="Periplasmic"
FT TRANSMEM 263..299
FT /note="Helical; Name=VI"
FT TOPO_DOM 300..303
FT /note="Cytoplasmic"
FT TRANSMEM 304..331
FT /note="Helical; Name=VII"
FT TOPO_DOM 332
FT /note="Periplasmic"
FT TRANSMEM 333..364
FT /note="Helical; Name=VIII"
FT TOPO_DOM 365..369
FT /note="Cytoplasmic"
FT TRANSMEM 370..395
FT /note="Helical; Name=IX"
FT TOPO_DOM 396..404
FT /note="Periplasmic"
FT TRANSMEM 405..437
FT /note="Helical; Name=X"
FT TOPO_DOM 438..440
FT /note="Cytoplasmic"
FT TRANSMEM 441..469
FT /note="Helical; Name=XI"
FT TOPO_DOM 470..478
FT /note="Periplasmic"
FT TRANSMEM 479..514
FT /note="Helical; Name=XII"
FT TOPO_DOM 515..558
FT /note="Cytoplasmic"
FT BINDING 94
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 276
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 280
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 325
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 326
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 411
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 413
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT DISULFID 66..80
FT CROSSLNK 276..280
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 28..57
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7ATE"
FT HELIX 84..101
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 128..150
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 178..206
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 219..250
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1QLE"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 264..298
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:3HB3"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:7AU6"
FT HELIX 334..345
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 371..394
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1QLE"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 420..436
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:3EHB"
FT HELIX 442..460
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 462..468
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:3HB3"
FT HELIX 483..513
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:3EHB"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:3HB3"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:1QLE"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:7ATE"
SQ SEQUENCE 558 AA; 62439 MW; A8402453C0C0339E CRC64;
MADAAVHGHG DHHDTRGFFT RWFMSTNHKD IGILYLFTAG IVGLISVCFT VYMRMELQHP
GVQYMCLEGA RLIADASAEC TPNGHLWNVM ITYHGVLMMF FVVIPALFGG FGNYFMPLHI
GAPDMAFPRL NNLSYWMYVC GVALGVASLL APGGNDQMGS GVGWVLYPPL STTEAGYSMD
LAIFAVHVSG ASSILGAINI ITTFLNMRAP GMTLFKVPLF AWSVFITAWL ILLSLPVLAG
AITMLLMDRN FGTQFFDPAG GGDPVLYQHI LWFFGHPEVY IIILPGFGII SHVISTFAKK
PIFGYLPMVL AMAAIGILGF VVWAHHMYTA GMSLTQQAYF MLATMTIAVP TGIKVFSWIA
TMWGGSIEFK TPMLWAFGFL FLFTVGGVTG VVLSQAPLDR VYHDTYYVVA HFHYVMSLGA
VFGIFAGVYY WIGKMSGRQY PEWAGQLHFW MMFIGSNLIF FPQHFLGRQG MPRRYIDYPV
EFAYWNNISS IGAYISFASF LFFIGIVFYT LFAGKRVNVP NYWNEHADTL EWTLPSPPPE
HTFETLPKRE DWDRAHAH
