ID M4NCV3_9GAMM Unreviewed; 463 AA.
AC M4NCV3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Cytochrome c, mono-and diheme variants family {ECO:0000313|EMBL:AGG87268.1};
DE Flags: Precursor;
GN ORFNames=R2APBS1_0083 {ECO:0000313|EMBL:AGG87268.1};
OS Rhodanobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG87268.1, ECO:0000313|Proteomes:UP000011859};
RN [1] {ECO:0000313|EMBL:AGG87268.1, ECO:0000313|Proteomes:UP000011859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2APBS1 {ECO:0000313|EMBL:AGG87268.1,
RC ECO:0000313|Proteomes:UP000011859};
RG US DOE Joint Genome Institute;
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT "Complete genome of Rhodanobacter sp. 2APBS1.";
RL Submitted (APR-2012) 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};
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DR EMBL; CP003470; AGG87268.1; -; Genomic_DNA.
DR RefSeq; WP_015446406.1; NZ_CP088918.1.
DR AlphaFoldDB; M4NCV3; -.
DR STRING; 666685.R2APBS1_0083; -.
DR KEGG; rhd:R2APBS1_0083; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_028594_0_0_6; -.
DR OrthoDB; 9811281at2; -.
DR Proteomes; UP000011859; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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; 2.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000018-51}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..463
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004056087"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..131
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 174..283
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 316..404
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 42
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 45
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 46
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 189
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 192
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 193
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 329
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 332
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 333
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 463 AA; 49280 MW; C152274D269C18EE CRC64;
MNVSTCGRLL LALLVTASAH AADTTDTTLL QRGQYLATAG DCVACHTAPG GKPYAGGLTV
PTPVGNIIST NITPSTTAGI GRYTEPQFRD ALRKGIRADG AHLYPAMPYT SYAQVTDDDV
RALYAYFMHG VASVDNRPAL TRLPFPFNLR LSMAGWNLLF LDRKPFTPDP AKDAKWNRGA
YLVRGLAHCS TCHTPRNLLM AERSSRELAG GMVGSWLAPN ITADANSGIG GWSEQDLVDY
LQLGHARGKA QAAGPMAEAV EHSLQHFEPA DLQAIASYLK TVPARHDPAD TRAVGGWGAA
FDGMADQRGI APPADAEQWS GEQLYDAHCA SCHQAGGEGS FDGGLPPLFH NTATGRVASG
NLVLVILEGI RWQTGDSGVH MPGFAGDLSD QQIATLGNYL TLRYGNPAAR ITATRVANLR
AGGAPSHLAA LVRLAMVVVV VLILAIIVLW RRRKRRRTSS GQA
//
