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Database: UniProt
Entry: F5SWR8_9GAMM
LinkDB: F5SWR8_9GAMM
Original site: F5SWR8_9GAMM 
ID   F5SWR8_9GAMM            Unreviewed;       194 AA.
AC   F5SWR8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Cytochrome c, mono-and diheme variant {ECO:0000313|EMBL:EGL54515.1};
GN   ORFNames=MAMP_01204 {ECO:0000313|EMBL:EGL54515.1};
OS   Methylophaga aminisulfidivorans MP.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL54515.1, ECO:0000313|Proteomes:UP000003544};
RN   [1] {ECO:0000313|EMBL:EGL54515.1, ECO:0000313|Proteomes:UP000003544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX   PubMed=21685284; DOI=10.1128/JB.05403-11;
RA   Han G.H., Kim W., Chun J., Kim S.W.;
RT   "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL   J. Bacteriol. 193:4265-4265(2011).
RN   [2] {ECO:0007829|PDB:7C90}
RP   X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) IN COMPLEX WITH HEME C.
RX   PubMed=32627749; DOI=10.4014/jmb.2006.06029;
RA   Ghosh S., Dhanasingh I., Ryu J., Kim S.W., Lee S.H.;
RT   "Crystal Structure of Cytochrome <i>c</i><sub>L</sub> from the Aquatic
RT   Methylotrophic Bacterium <i>Methylophaga aminisulfidivorans</i>
RT   MP<sup>T</sup>.";
RL   J. Microbiol. Biotechnol. 30:1261-1271(2020).
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000008-1}.
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:EGL54515.1}.
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DR   EMBL; AFIG01000001; EGL54515.1; -; Genomic_DNA.
DR   RefSeq; WP_007144401.1; NZ_AFIG01000001.1.
DR   PDB; 7C90; X-ray; 2.13 A; A/B/C/D=1-194.
DR   AlphaFoldDB; F5SWR8; -.
DR   SMR; F5SWR8; -.
DR   STRING; 1026882.MAMP_01204; -.
DR   eggNOG; COG2010; Bacteria.
DR   OrthoDB; 9811281at2; -.
DR   Proteomes; UP000003544; 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; 1.10.760.10; Cytochrome c-like domain; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR009153; Cyt_cL.
DR   NCBIfam; TIGR03872; cytochrome_MoxG; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PIRSF; PIRSF000008; Cytochrome_c551i; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:7C90};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000008-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000008-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000008-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT   DOMAIN          75..155
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         88
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_note="covalent"
FT                   /evidence="ECO:0007829|PDB:7C90"
FT   BINDING         88
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000008-1"
FT   BINDING         91
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_note="covalent"
FT                   /evidence="ECO:0007829|PDB:7C90"
FT   BINDING         91
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000008-1"
FT   BINDING         92
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:7C90"
FT   BINDING         92
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000008-2"
FT   BINDING         110
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /evidence="ECO:0007829|PDB:7C90"
FT   BINDING         111
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /evidence="ECO:0007829|PDB:7C90"
FT   BINDING         114
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /evidence="ECO:0007829|PDB:7C90"
FT   BINDING         129
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /evidence="ECO:0007829|PDB:7C90"
FT   BINDING         132
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /ligand_part_note="axial binding residue"
FT                   /evidence="ECO:0007829|PDB:7C90"
SQ   SEQUENCE   194 AA;  21594 MW;  7B0A513E40FEF220 CRC64;
     MTIKTFLPKK IRGIALLTVS VLSVVMIPVA QSQLVFRNTV TGDVLDLSFG KKGEKTEAVE
     HFLNTGENLY NTDDEAIKAG ESLFMTACSG CHGHHAEGKL GPALGDDYYT YPKNANDKGL
     FETIYGGARS MMGPQYNNLT KDEILHIMAW VRSVYWGSAD KADWLTEEQK ANFKPAEVPE
     DFKEAMDNFN KTHH
//
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