ID A0A176F3U3_9RHOB Unreviewed; 341 AA.
AC A0A176F3U3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cytochrome B {ECO:0000313|EMBL:KZY34234.1};
GN ORFNames=A3731_03010 {ECO:0000313|EMBL:KZY34234.1};
OS Roseovarius sp. HI0049.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1822235 {ECO:0000313|EMBL:KZY34234.1, ECO:0000313|Proteomes:UP000077043};
RN [1] {ECO:0000313|EMBL:KZY34234.1, ECO:0000313|Proteomes:UP000077043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0049 {ECO:0000313|EMBL:KZY34234.1,
RC ECO:0000313|Proteomes:UP000077043};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00029368};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000256|ARBA:ARBA00007866}.
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:KZY34234.1}.
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DR EMBL; LWFA01002894; KZY34234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176F3U3; -.
DR Proteomes; UP000077043; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR CDD; cd04213; CuRO_CcO_Caa3_II; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034236; CuRO_CcO_Caa3_II.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1.
DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..238
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT DOMAIN 249..341
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 341 AA; 37152 MW; 80D3CB0CC1F394A8 CRC64;
MSSRQRDRGH HWLLGPAGVK LAGFLTLALL PGCGKEQSAL DAAGVDAEAI LNIFLVTLVG
ACILWLLVNG AFYTLTRLRT GPMDERFVRP LLIGGGIVAP SIILVALLVW ALSILPDQRA
PGHGLQVRVT GEQWWWRVEY WPEGAEEPVV TANEIRLPAG QRTEFLLGAD RVIHSFWIPS
LGGKMDMFPG KETRVSLHPE RPGRYRGQCA EFCGASHAWM AFAAVVMPEE EFDAWLEREA
GEAAAPESAG AMRGEELFRS EGCGACHAVR GTEAVGQVGP DLTHVGSRET LGAGRLGTTL
EDFERWIAHT GELKPEVRMP TYDHLGEAEI ADLAAYLKGL K
//
