ID D4BA38_9ENTR Unreviewed; 402 AA.
AC D4BA38;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Cytochrome C {ECO:0000313|EMBL:EFE09049.1};
GN ORFNames=CIT292_07330 {ECO:0000313|EMBL:EFE09049.1};
OS Citrobacter youngae ATCC 29220.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=500640 {ECO:0000313|EMBL:EFE09049.1, ECO:0000313|Proteomes:UP000003880};
RN [1] {ECO:0000313|EMBL:EFE09049.1, ECO:0000313|Proteomes:UP000003880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29220 {ECO:0000313|EMBL:EFE09049.1,
RC ECO:0000313|Proteomes:UP000003880};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000256|PIRSR:PIRSR000018-50};
CC Note=Binds 3 heme c groups covalently per subunit.
CC {ECO:0000256|PIRSR:PIRSR000018-50};
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:EFE09049.1}.
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DR EMBL; ABWL02000006; EFE09049.1; -; Genomic_DNA.
DR RefSeq; WP_006684727.1; NZ_GG730299.1.
DR AlphaFoldDB; D4BA38; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_028594_0_0_6; -.
DR Proteomes; UP000003880; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR PANTHER; PTHR35008:SF8; BLL4482 PROTEIN; 1.
DR PANTHER; PTHR35008; BLL4482 PROTEIN-RELATED; 1.
DR Pfam; PF00034; Cytochrom_C; 2.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR SUPFAM; SSF46626; Cytochrome c; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000018-50};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000018-51};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000018-51}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003054800"
FT DOMAIN 18..121
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 168..275
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 293..382
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 32
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 35
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 36
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:PIRSR000018-51"
FT BINDING 183
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 186
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 187
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:PIRSR000018-51"
FT BINDING 306
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 309
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-50"
FT BINDING 310
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000018-51"
SQ SEQUENCE 402 AA; 43032 MW; 74DB41E62790391F CRC64;
MRNVTVLAAC LFTASVSAAE SDGEYIARIS DCVACHTTEG GAAMAGGKKF PTPVGDIYST
NITPDKAQGI GNYAYEDFEK AVRQGIAKDG HPLYPAMPYP SYAKLSDDDV QALYRYFMHD
VTPSAQPNKE NAIPWLLSAR WPLHIWNWLF TDAPAATVES ENTGDNAALV KRGAYLVEGP
GHCGSCHTPR GMAMNEKAYS NADPEYLSGA MIDGWYAPSL RGSGMSEQAL KSLLLTGKSK
HAAVSGSMAE VVTQSTQYLT DEDATAIAQY LLSLKSAKPE AGRTAAATVA WSSSAEAGKV
TYNRYCSTCH GLEGKGTDDN APSLNNNPLV MVDDPTPLYR VIAHGAETPT TRGSVSFKMP
AYNGVLSDSE MRDVINYLRK SWGEGNGEVS QEDLAGVKKA SH
//
