CY550_PSEAE
ID CY550_PSEAE Reviewed; 145 AA.
AC Q9I2C5; Q7B310;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cytochrome c550 {ECO:0000303|PubMed:10075429};
DE Flags: Precursor;
GN Name=exaB {ECO:0000303|PubMed:10075429, ECO:0000312|EMBL:AAG05371.1,
GN ECO:0000312|EMBL:CAA08895.1};
GN OrderedLocusNames=PA1983 {ECO:0000312|EMBL:AAG05371.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-57, FUNCTION,
RP HEME-BINDING, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, PATHWAY, AND
RP INDUCTION.
RC STRAIN=ATCC 17933;
RX PubMed=10075429; DOI=10.1099/13500872-145-2-471;
RA Schobert M., Goerisch H.;
RT "Cytochrome c550 is an essential component of the quinoprotein ethanol
RT oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the
RT genes encoding cytochrome c550 and an adjacent acetaldehyde
RT dehydrogenase.";
RL Microbiology 145:471-481(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RC STRAIN=ATCC 17933;
RX PubMed=9826187; DOI=10.1046/j.1432-1327.1998.2570409.x;
RA Diehl A., von Wintzingerode F., Gorisch H.;
RT "Quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa is a
RT homodimer: sequence of the gene and deduced structural properties of the
RT enzyme.";
RL Eur. J. Biochem. 257:409-419(1998).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, HEME-BINDING, AND
RP SUBUNIT.
RC STRAIN=ATCC 17933;
RX PubMed=8380982; DOI=10.1042/bj2890173;
RA Reichmann P., Goerisch H.;
RT "Cytochrome c550 from Pseudomonas aeruginosa.";
RL Biochem. J. 289:173-178(1993).
RN [5]
RP INTERACTION WITH EXAA.
RC STRAIN=ATCC 17933;
RX PubMed=19224199; DOI=10.1007/s00203-009-0460-4;
RA Mennenga B., Kay C.W., Goerisch H.;
RT "Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the
RT unusual disulfide ring formed by adjacent cysteine residues is essential
RT for efficient electron transfer to cytochrome c550.";
RL Arch. Microbiol. 191:361-367(2009).
CC -!- FUNCTION: Is an essential component of the ethanol oxidation system
CC that allows P.aeruginosa to grow on ethanol as the sole carbon and
CC energy source. Is the direct electron acceptor of the quinoprotein
CC ethanol dehydrogenase (QEDH). {ECO:0000269|PubMed:10075429,
CC ECO:0000269|PubMed:8380982}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is 280 mV. {ECO:0000269|PubMed:8380982};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol.
CC {ECO:0000269|PubMed:10075429}.
CC -!- SUBUNIT: Monomer (PubMed:8380982). Interacts with the quinoprotein
CC ethanol dehydrogenase (QEDH) ExaA (PubMed:19224199).
CC {ECO:0000269|PubMed:19224199, ECO:0000269|PubMed:8380982}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10075429}.
CC -!- INDUCTION: Induced by growth on ethanol. {ECO:0000269|PubMed:8380982,
CC ECO:0000305|PubMed:10075429}.
CC -!- PTM: Binds 1 heme group per subunit. {ECO:0000269|PubMed:10075429,
CC ECO:0000269|PubMed:8380982}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are completely unable to
CC grow on ethanol as the sole carbon source.
CC {ECO:0000269|PubMed:10075429}.
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; AF068264; AAC79658.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05371.1; -; Genomic_DNA.
DR EMBL; AJ009858; CAA08895.1; -; Genomic_DNA.
DR PIR; G83396; G83396.
DR RefSeq; NP_250673.1; NC_002516.2.
DR RefSeq; WP_003113462.1; NZ_QZGE01000030.1.
DR AlphaFoldDB; Q9I2C5; -.
DR SMR; Q9I2C5; -.
DR STRING; 287.DR97_5864; -.
DR PaxDb; Q9I2C5; -.
DR DNASU; 880387; -.
DR EnsemblBacteria; AAG05371; AAG05371; PA1983.
DR GeneID; 880387; -.
DR KEGG; pae:PA1983; -.
DR PATRIC; fig|208964.12.peg.2067; -.
DR PseudoCAP; PA1983; -.
DR HOGENOM; CLU_084762_1_0_6; -.
DR OMA; HGNVTPQ; -.
DR BioCyc; PAER208964:G1FZ6-2021-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 GO; GO:0006069; P:ethanol oxidation; IMP:PseudoCAP.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR030991; c550_PedF.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR TIGRFAMs; TIGR04494; c550_PedF; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:10075429"
FT CHAIN 25..145
FT /note="Cytochrome c550"
FT /id="PRO_5004326969"
FT DOMAIN 60..142
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 73
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 76
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 77
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 119
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 /evidence="ECO:0000305|PubMed:10075429"
FT CONFLICT 6
FT /note="V -> A (in Ref. 3; CAA08895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 15850 MW; 06C1E1BB326B8B32 CRC64;
MNKNNVLRGL LVLAGLSLSS LALAHGDVTP QAVDTKGLEP LGKEWRDTNP YRKPYAKHDL
AVEIGASAYN QNCARCHGLE AKSGGIAPDL RLLETGAEGD EWFKERVING AVRDGAVYMP
KMADFISQEG LWAIRSYLES VHVDE
