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Database: UniProt
Entry: G7GF28_9GAMM
LinkDB: G7GF28_9GAMM
Original site: G7GF28_9GAMM 
ID   G7GF28_9GAMM            Unreviewed;       129 AA.
AC   G7GF28;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Putative cytochrome b {ECO:0000313|EMBL:GAB02203.1};
GN   ORFNames=ACT4_026_00110 {ECO:0000313|EMBL:GAB02203.1};
OS   Acinetobacter sp. NBRC 100985.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1071390 {ECO:0000313|EMBL:GAB02203.1, ECO:0000313|Proteomes:UP000012044};
RN   [1] {ECO:0000313|EMBL:GAB02203.1, ECO:0000313|Proteomes:UP000012044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100985 {ECO:0000313|EMBL:GAB02203.1,
RC   ECO:0000313|Proteomes:UP000012044};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Acinetobacter sp. NBRC 100985.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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:GAB02203.1}.
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DR   EMBL; BAEB01000026; GAB02203.1; -; Genomic_DNA.
DR   RefSeq; WP_007482110.1; NZ_BAEB01000026.1.
DR   AlphaFoldDB; G7GF28; -.
DR   Proteomes; UP000012044; Unassembled WGS sequence.
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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..129
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003494990"
FT   BINDING         30
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         125
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   129 AA;  14154 MW;  7AA836BDA8CC4151 CRC64;
     MNKRILMCAL VSGSLFLSQA VSAHQLEKDM HVLAKTMTVF AQTDDLAEAN KQLALMRKAA
     VSSKASLPHQ LEGLAPENDQ VKSYQGGLDQ LIAEIDAVTA LVAKGQLEDA KVEALKLVKL
     RNEYHQHFK
//
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