ID A0A2A7UZ84_COMTR Unreviewed; 459 AA.
AC A0A2A7UZ84;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cytochrome C {ECO:0000313|EMBL:PEH90567.1};
GN ORFNames=CRM82_19945 {ECO:0000313|EMBL:PEH90567.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH90567.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) 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:PEH90567.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDEA01000001; PEH90567.1; -; Genomic_DNA.
DR RefSeq; WP_066537086.1; NZ_UIGV01000001.1.
DR AlphaFoldDB; A0A2A7UZ84; -.
DR STRING; 1219032.GCA_001515545_02103; -.
DR GeneID; 80802907; -.
DR OrthoDB; 9809720at2; -.
DR Proteomes; UP000220246; 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; IPR008168; Cyt_C_IC.
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; 3.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR PRINTS; PR00605; CYTCHROMECIC.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000220246}.
FT DOMAIN 42..145
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 188..300
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 340..430
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 437..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56
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 59
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 60
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 203
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 206
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 207
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 353
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 356
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 357
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 459 AA; 49107 MW; 1EB759511C53EF83 CRC64;
MKKILSILIA LIVLGIVAAL ALAYAPFKPT PANETLAADW KAEPGRGEYV MRAGDCMACH
TANGGESMAG GRGIESPLGT IWSSNITPDK ETGIGNWTLD QFRAAMVDGV GGHGQQLYPA
MPYENYRFMT ESDLRALYDY IQTEVKPVKN EVQATSLTFP FNMRFGLRAW NWLALSGEAK
FKPMAGDEQQ IRGQYLVEGA GHCAACHSPR TTFMAQDGTR LSDASFLTGG MVDEWTAPAL
RGKDARVQKW TAEEIAAYLA TGRNAHAVAN GEMALVVEHS MQYMTDADLN AMAVFLKSMD
GQPVEAVPAK VAAAGPRSMP ALPADEAGKA TATLLTSASP DMPVGARLYL DNCAACHFVS
GKGAPEIFPE LQGNAMVLGK DANPFVSVIL NGTSVPSTSR RPMHLAMQGY ADRLTDEEVA
QLASFIRNGW GNKASNVSAS DVSKVRKHTQ AAAAPERAQ
//
