ID   CYB5_ECTSH              Reviewed;          91 AA.
AC   P82291;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Soluble cytochrome b558;
OS   Ectothiorhodospira shaposhnikovii (Ectothiorhodospira vacuolata).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=1054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-91, X-RAY
RP   CRYSTALLOGRAPHY (1.65 ANGSTROMS), DISULFIDE BOND, AND MASS SPECTROMETRY.
RX   PubMed=10585439; DOI=10.1074/jbc.274.50.35614;
RA   Kostanjevecki V., Leys D., Van Driessche G., Meyer T.E., Cusanovich M.A.,
RA   Fischer U., Guisez Y., Van Beeumen J.;
RT   "Structure and characterization of Ectothiorhodospira vacuolata cytochrome
RT   b(558), a prokaryotic homologue of cytochrome b(5).";
RL   J. Biol. Chem. 274:35614-35620(1999).
CC   -!- MASS SPECTROMETRY: Mass=10094.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10585439};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR   EMBL; AF183259; AAD56233.1; -; Genomic_DNA.
DR   PDB; 1CXY; X-ray; 1.65 A; A=2-91.
DR   PDBsum; 1CXY; -.
DR   AlphaFoldDB; P82291; -.
DR   SMR; P82291; -.
DR   EvolutionaryTrace; P82291; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.120.10; -; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Heme; Iron; Metal-binding; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10585439"
FT   CHAIN           2..91
FT                   /note="Soluble cytochrome b558"
FT                   /id="PRO_0000166037"
FT   DOMAIN          8..88
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         43
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         71
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   DISULFID        25..54
FT                   /evidence="ECO:0000269|PubMed:10585439"
FT   HELIX           13..16
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   STRAND          32..35
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   HELIX           59..64
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   TURN            65..68
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   HELIX           73..81
FT                   /evidence="ECO:0007829|PDB:1CXY"
FT   STRAND          83..86
FT                   /evidence="ECO:0007829|PDB:1CXY"
SQ   SEQUENCE   91 AA;  10229 MW;  ABBAF71EC58FB1ED CRC64;
     MNETEATLPV FTLEQVAEHH SPDDCWMAIH GKVYDLTPYV PNHPGPAGMM LVWCGQESTE
     AWETKSYGEP HSSLAARLLQ RYLIGTLEEI T