ID Q6F800_ACIAD Unreviewed; 137 AA.
AC Q6F800;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Putative of Cytochrome b(562) (CybC) {ECO:0000313|EMBL:CAG69815.1};
GN OrderedLocusNames=ACIAD3123 {ECO:0000313|EMBL:CAG69815.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG69815.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG69815.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|PIRSR:PIRSR000029-1};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per molecule.
CC {ECO:0000256|PIRSR:PIRSR000029-1};
CC -!- SIMILARITY: Belongs to the cytochrome b562 family.
CC {ECO:0000256|ARBA:ARBA00005523}.
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DR EMBL; CR543861; CAG69815.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F800; -.
DR STRING; 202950.GCA_001485005_02775; -.
DR KEGG; aci:ACIAD3123; -.
DR eggNOG; COG3783; Bacteria.
DR HOGENOM; CLU_140814_0_0_6; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.20.120.10; Cytochrome c/b562; 1.
DR InterPro; IPR009155; Cyt_b562.
DR InterPro; IPR010980; Cyt_c/b562.
DR Pfam; PF07361; Cytochrom_B562; 1.
DR PIRSF; PIRSF000029; Cytochrome_b562; 1.
DR SUPFAM; SSF47175; Cytochromes; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR000029-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000029-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000029-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..137
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004273180"
FT BINDING 38
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000029-1"
FT BINDING 133
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000029-1"
SQ SEQUENCE 137 AA; 14866 MW; 3499A19114537967 CRC64;
MHINGSQSMN KKILGSILLI GSLSVSHLAM AASLQNNMIS IATAYSDFSK SSNVKDAETA
LNKMKLAAID SQKSKPSKLA NKPDNSAEVM DYHKGLDQLV AEIDKTNLLV KAGKLDQAKV
EGKTLLDIRN VNHKKFK
//
