ID U3LTB8_9STRA Unreviewed; 195 AA.
AC U3LTB8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 22-APR-2020, entry version 24.
DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457};
DE Flags: Fragment;
GN Name=COX2 {ECO:0000313|EMBL:AGK25033.1};
OS Pythium nagaii.
OG Mitochondrion {ECO:0000313|EMBL:AGK25033.1}.
OC Eukaryota; Sar; Stramenopiles; Oomycetes; Pythiales; Pythiaceae; Pythium.
OX NCBI_TaxID=289625 {ECO:0000313|EMBL:AGK25033.1};
RN [1] {ECO:0000313|EMBL:AGK25033.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P16712 {ECO:0000313|EMBL:AGK25033.1};
RX PubMed=23709523; DOI=10.3852/12-322;
RA Bahramisharif A., Lamprecht S.C., Spies C.F., Botha W.J., McLeod A.;
RT "Pythium cederbergense sp. nov. and related taxa from Pythium clade G
RT associated with the South African indigenous plant Aspalathus linearis
RT (rooibos).";
RL Mycologia 105:1174-1189(2013).
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:0000256|RuleBase:RU000457}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c]
CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-
CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|SAAS:SAAS01246709};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000457};
CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU000457}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000256|RuleBase:RU000457}.
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DR EMBL; JX397984; AGK25033.1; -; Genomic_DNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR CDD; cd13912; CcO_II_C; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR034210; CcO_II_C.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709548};
KW Electron transport {ECO:0000256|RuleBase:RU000457,
KW ECO:0000256|SAAS:SAAS00709556};
KW Membrane {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00883094,
KW ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000457,
KW ECO:0000256|SAAS:SAAS00709462};
KW Mitochondrion {ECO:0000256|RuleBase:RU000457, ECO:0000313|EMBL:AGK25033.1};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457};
KW Oxidoreductase {ECO:0000256|SAAS:SAAS01246698};
KW Respiratory chain {ECO:0000256|RuleBase:RU000457,
KW ECO:0000256|SAAS:SAAS00709567};
KW Transmembrane {ECO:0000256|RuleBase:RU000457,
KW ECO:0000256|SAAS:SAAS00882981, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAAS:SAAS00883111,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709552}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..85
FT /note="COX2_TM"
FT /evidence="ECO:0000259|PROSITE:PS50999"
FT DOMAIN 86..195
FT /note="COX2_CUA"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGK25033.1"
FT NON_TER 195
FT /evidence="ECO:0000313|EMBL:AGK25033.1"
SQ SEQUENCE 195 AA; 22258 MW; B9E9F027B274F643 CRC64;
PATPVMEGII NFHHDLMFFL IVVTIFVCWM LFRVITLFDE KKNKIPSTVV HGATIEIIWT
SVPALILLTV AVPSFALLYS MDEVIDPIIT LKVIGSQWYW SYEYSDNLEF SDEPLIFDSY
MVQENDLEIG QFRLLEVDNR VVVPTNSHIR VLITASDVLH SWAIPSLGIK LDACPGRLNQ
TSMFIKREGV FYGQC
//