ID A0A0T2QIF2_9SPHN Unreviewed; 551 AA.
AC A0A0T2QIF2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN ORFNames=ASD76_11085 {ECO:0000313|EMBL:KRA84488.1};
OS Altererythrobacter sp. Root672.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA84488.1, ECO:0000313|Proteomes:UP000051125};
RN [1] {ECO:0000313|EMBL:KRA84488.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA84488.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA84488.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA84488.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC Note=Binds 1 copper ion per subunit, denoted as copper B.
CC {ECO:0000256|PIRSR:PIRSR604677-50};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC Note=Binds 2 heme groups per subunit, denoted as high- and low-spin.
CC {ECO:0000256|PIRSR:PIRSR604677-50};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000370}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRA84488.1}.
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DR EMBL; LMHH01000001; KRA84488.1; -; Genomic_DNA.
DR RefSeq; WP_055922581.1; NZ_LMHH01000001.1.
DR AlphaFoldDB; A0A0T2QIF2; -.
DR STRING; 1736584.ASD76_11085; -.
DR OrthoDB; 9806838at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000051125; Unassembled WGS sequence.
DR GO; GO:0045278; C:plasma membrane 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01661; cbb3_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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 NCBIfam; TIGR00780; ccoN; 1.
DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR10422:SF29; CYTOCHROME C OXIDASE SUBUNIT 1 HOMOLOG, BACTEROID; 1.
DR Pfam; PF00115; COX1; 1.
DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|RuleBase:RU000370};
KW Heme {ECO:0000256|PIRSR:PIRSR604677-50, ECO:0000256|RuleBase:RU000370};
KW Iron {ECO:0000256|PIRSR:PIRSR604677-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR604677-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000051125};
KW Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000370};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000370}.
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 266..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..551
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT BINDING 121
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:0000256|PIRSR:PIRSR604677-50"
FT BINDING 270
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 320
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 321
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT BINDING 408
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:0000256|PIRSR:PIRSR604677-50"
FT BINDING 410
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:0000256|PIRSR:PIRSR604677-50"
SQ SEQUENCE 551 AA; 61792 MW; B31BD0DFDEE35976 CRC64;
MDTVVARTGF WFVVILLAIV AVALSQDAGY AAHMTIVALA AGVCLVVSMT NVDYTAVANG
ILRVPADPSR YDDDPIRWGV IATVFWGIVG FLAGVFIALQ LAYPQLNFEP YLNFGRVRPL
HTSAVIFAFG GNALIATSFY VVQRTCRARL AFPQLARFVF WGYQLFIVLA ASGYLLGVTQ
SKEYAEPEWY VDWWLTIVWL AYLAVFVGTI IKRSEPHIYV ANWFYLAFII TVAMLHVVNN
LDMPVSLLGS KSYPLFAGVQ GALVQWWYGH NAVGFFLTAG FLAMMYYFVP KQAERPIYSY
RLSIIHFWSL IFLYIWAGPH HLHYTALPDW AQTLGMVFSI MLWMPSWGGM INGLMTLNGA
WDKIRTDPII RMMVMSLAFY GMSTFEGPLM SIKSVNSLSH YTDWTIGHVH SGALGWNGLI
TFAAVYYLVP RLWGRERLYS LRMVNWHFWL ATMGIVFYAG SMWVAGITQG LMWREFGADG
YLVNSFADTV AALHPMYALR AVGGALYLAG GLVMVWNVWA TILGRLRTEA PMSDAAFDPA
KDRPIVAVPA E
//
