CYCA_METME
ID CYCA_METME Reviewed; 144 AA.
AC Q9RQB9; Q9R555;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cytochrome c'';
DE Flags: Precursor;
GN Name=cycA;
OS Methylophilus methylotrophus (Bacterium W3A1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=17 {ECO:0000312|EMBL:AAF13764.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AS4 / NCIMB 11585;
RX PubMed=10524262; DOI=10.1016/s0005-2728(99)00085-7;
RA Price N.J., Vijgenboom E., Ribeiro G., Costa J.V., Canters G.W., Santos H.;
RT "Cloning and sequence analysis of the gene encoding Methylophilus
RT methylotrophus cytochrome c'', a unique protein with a perpendicular
RT orientation of the histidinyl ligands.";
RL Biochim. Biophys. Acta 1413:55-61(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 21-144, AND MASS SPECTROMETRY.
RX PubMed=10354493; DOI=10.1016/s0005-2728(99)00050-x;
RA Klarskov K., Leys D., Backers K., Costa H.S., Santos H., Guisez Y.,
RA Van Beeumen J.J.;
RT "Cytochrome c'' from the obligate methylotroph Methylophilus
RT methylotrophus, an unexpected homolog of sphaeroides heme protein from the
RT phototroph Rhodobacter sphaeroides.";
RL Biochim. Biophys. Acta 1412:47-55(1999).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 21-82.
RX PubMed=8394812; DOI=10.1111/j.1432-1033.1993.tb18097.x;
RA Costa H.S., Santos H., Turner D.L.;
RT "Characterization of the haem environment in Methylophilus methylotrophus
RT ferricytochrome c'' by 1H-NMR.";
RL Eur. J. Biochem. 215:817-824(1993).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 21-64, AND SUBUNIT.
RA Santos H., Turner D.L.;
RT "Characterization and NMR studies of a novel cytochrome c isolated from
RT Methylophilus methylotrophus which shows a redox-linked change of spin
RT state.";
RL Biochim. Biophys. Acta 954:277-286(1988).
RN [5] {ECO:0000305}
RP CHARACTERIZATION.
RC STRAIN=ATCC 53528 / AS1 / DSM 46235 / LMG 6787 / NCIMB 10515;
RX PubMed=1325909; DOI=10.1111/j.1432-1033.1992.tb17204.x;
RA Costa H.S., Santos H., Turner D.L., Xavier A.V.;
RT "Involvement of a labile axial histidine in coupling electron and proton
RT transfer in Methylophilus methylotrophus cytochrome c''.";
RL Eur. J. Biochem. 208:427-433(1992).
RN [6] {ECO:0000305}
RP EPR SPECTROSCOPY.
RX PubMed=2169241; DOI=10.1042/bj2700413;
RA Berry M.J., George S.J., Thomson A.J., Santos H., Turner D.L.;
RT "Cytochrome c'' isolated from Methylophilus methylotrophus. An example of
RT bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation
RT of the ligands.";
RL Biochem. J. 270:413-417(1990).
RN [7] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) OF 21-144.
RX PubMed=12595732; DOI=10.1107/s0907444903001045;
RA Enguita F.J., Rodrigues L., Archer M., Sieker L., Rodrigues A., Pohl E.,
RA Turner D.L., Santos H., Carrondo M.A.;
RT "Crystallization and preliminary X-ray characterization of cytochrome c''
RT from the obligate methylotroph Methylophilus methylotrophus.";
RL Acta Crystallogr. D 59:580-583(2003).
RN [8] {ECO:0000305}
RP STRUCTURE BY NMR OF 21-144.
RX PubMed=11327772; DOI=10.1006/jmbi.2001.4600;
RA Brennan L., Turner D.L., Fareleira P., Santos H.;
RT "Solution structure of Methylophilus methylotrophus cytochrome c'':
RT insights into the structural basis of haem-ligand detachment.";
RL J. Mol. Biol. 308:353-365(2001).
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.4, ECO:0000305}.
CC -!- PTM: Binds 1 heme c group covalently per subunit. The heme is low-spin
CC in the oxidized state but switches to a high-spin form upon reduction,
CC due to the dissociation of one of the axial histidines, His-115.
CC -!- MASS SPECTROMETRY: Mass=14292.9; Mass_error=1.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10354493};
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DR EMBL; AF119838; AAF13764.1; -; Genomic_DNA.
DR PIR; S35046; S35046.
DR PDB; 1E8E; NMR; -; A=21-144.
DR PDB; 1GU2; X-ray; 1.19 A; A/B=21-144.
DR PDB; 1OAE; X-ray; 1.95 A; A/B=21-144.
DR PDBsum; 1E8E; -.
DR PDBsum; 1GU2; -.
DR PDBsum; 1OAE; -.
DR AlphaFoldDB; Q9RQB9; -.
DR BMRB; Q9RQB9; -.
DR SMR; Q9RQB9; -.
DR STRING; 1122236.KB905145_gene2474; -.
DR DrugBank; DB03317; Ferroheme C.
DR EvolutionaryTrace; Q9RQB9; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR015170; DUF1924.
DR Pfam; PF09086; DUF1924; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Heme; Iron; Metal-binding; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:10354493,
FT ECO:0000269|PubMed:8394812, ECO:0000269|Ref.4"
FT CHAIN 21..144
FT /note="Cytochrome c''"
FT /id="PRO_0000006512"
FT BINDING 69
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 72
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 73
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 BINDING 115
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 DISULFID 116..124
FT /evidence="ECO:0000269|PubMed:11327772"
FT HELIX 22..39
FT /evidence="ECO:0007829|PDB:1GU2"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:1GU2"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1E8E"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1E8E"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1E8E"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1GU2"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1GU2"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1GU2"
FT TURN 99..103
FT /evidence="ECO:0007829|PDB:1GU2"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:1GU2"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:1GU2"
SQ SEQUENCE 144 AA; 15792 MW; 4B9FFEE42D595D8D CRC64;
MKIKTIIAVF GVLFSAHALA DVTNAEKLVY KYTNIAHSAN PMYEAPSITD GKIFFNRKFK
TPSGKEAACA SCHTNNPANV GKNIVTGKEI PPLAPRVNTK RFTDIDKVED EFTKHCNDIL
GADCSPSEKA NFIAYLLTET KPTK
