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Database: UniProt
Entry: E1VMN6_9GAMM
LinkDB: E1VMN6_9GAMM
Original site: E1VMN6_9GAMM 
ID   E1VMN6_9GAMM            Unreviewed;       242 AA.
AC   E1VMN6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Cytochrome c family protein {ECO:0000313|EMBL:CBL46078.1};
GN   ORFNames=HDN1F_24950 {ECO:0000313|EMBL:CBL46078.1};
OS   gamma proteobacterium HdN1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL46078.1, ECO:0000313|Proteomes:UP000002677};
RN   [1] {ECO:0000313|EMBL:CBL46078.1, ECO:0000313|Proteomes:UP000002677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA   Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA   Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT   "Alkane degradation by a new type of denitrifying bacterium with possible
RT   involvement of the electron acceptor in substrate activation.";
RL   Environ. Microbiol. 0:0-0(2010).
CC   -!- PTM: Binds 2 heme c groups covalently per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000005-1}.
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DR   EMBL; FP929140; CBL46078.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1VMN6; -.
DR   STRING; 83406.HDN1F_24950; -.
DR   KEGG; gpb:HDN1F_24950; -.
DR   eggNOG; COG2863; Bacteria.
DR   HOGENOM; CLU_076280_0_1_6; -.
DR   OrthoDB; 9773456at2; -.
DR   Proteomes; UP000002677; 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; 1.10.760.10; Cytochrome c-like domain; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR024167; Cytochrome_c4-like.
DR   PANTHER; PTHR33751:SF11; BLL4483 PROTEIN; 1.
DR   PANTHER; PTHR33751; CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP; 1.
DR   Pfam; PF00034; Cytochrom_C; 2.
DR   PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000005-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000005-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000005-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002677};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..242
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003153005"
FT   DOMAIN          27..114
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          124..214
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         47
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         50
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         51
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         91
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         145
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         148
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-1"
FT   BINDING         149
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
FT   BINDING         191
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000005-2"
SQ   SEQUENCE   242 AA;  25895 MW;  BB32A0D45B618A0D CRC64;
     MKKQLFLGAL LSVVTVSSLA ASGASRNEVV NGEKIAREGN GRGAVGCLVC HGMHGEGVSV
     SGFPRLAGLN ARYLEKQLND FVSGARDNVV MKPTATALSE DERRAVADYY SKLSVPERVA
     ITLESNEVGE ALALRGKWDQ QVPACIQCHG PNGVGIGEHF PPLSGQSALY LANQMREWKK
     GSRANDPLGL MKHVAQSLTE SEILAVAKWF SSQPTFLVEN SDITSQVSAQ ETTQEKVTGG
     KQ
//
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