ID CYDA_ECOLI Reviewed; 522 AA.
AC P0ABJ9; P11026; P75754; P76823;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Cytochrome bd-I ubiquinol oxidase subunit 1;
DE EC=7.1.1.7 {ECO:0000269|PubMed:1850294, ECO:0000269|PubMed:6307994};
DE AltName: Full=Cytochrome bd-I oxidase subunit I;
DE AltName: Full=Cytochrome d ubiquinol oxidase subunit I;
GN Name=cydA; Synonyms=cyd-1; OrderedLocusNames=b0733, JW0722;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2843510; DOI=10.1016/s0021-9258(18)37682-8;
RA Green G.N., Fang H., Lin R.-J., Newton G., Mather M., Georgiou C.D.,
RA Gennis R.B.;
RT "The nucleotide sequence of the cyd locus encoding the two subunits of the
RT cytochrome d terminal oxidase complex of Escherichia coli.";
RL J. Biol. Chem. 263:13138-13143(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-6, FORMYLATION AT MET-1, AND SUBUNIT.
RC STRAIN=MR43L/F152;
RX PubMed=3281937; DOI=10.1016/s0021-9258(18)60705-7;
RA Miller M.J., Hermodson M., Gennis R.B.;
RT "The active form of the cytochrome d terminal oxidase complex of
RT Escherichia coli is a heterodimer containing one copy of each of the two
RT subunits.";
RL J. Biol. Chem. 263:5235-5240(1988).
RN [6]
RP FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP COFACTOR, SUBUNIT, AND INDUCTION.
RC STRAIN=MR43L/F152;
RX PubMed=6307994; DOI=10.1016/s0021-9258(17)44645-x;
RA Miller M.J., Gennis R.B.;
RT "The purification and characterization of the cytochrome d terminal oxidase
RT complex of the Escherichia coli aerobic respiratory chain.";
RL J. Biol. Chem. 258:9159-9165(1983).
RN [7]
RP COFACTOR.
RX PubMed=3013298; DOI=10.1021/bi00357a002;
RA Green G.N., Lorence R.M., Gennis R.B.;
RT "Specific overproduction and purification of the cytochrome b558 component
RT of the cytochrome d complex from Escherichia coli.";
RL Biochemistry 25:2309-2314(1986).
RN [8]
RP COFACTOR.
RC STRAIN=MR43L/F152;
RX PubMed=3013299; DOI=10.1021/bi00357a003;
RA Lorence R.M., Koland J.G., Gennis R.B.;
RT "Coulometric and spectroscopic analysis of the purified cytochrome d
RT complex of Escherichia coli: evidence for the identification of 'cytochrome
RT a1' as cytochrome b595.";
RL Biochemistry 25:2314-2321(1986).
RN [9]
RP TOPOLOGY.
RX PubMed=3138232; DOI=10.1016/s0021-9258(18)37681-6;
RA Georgiou C.D., Dueweke T.J., Gennis R.B.;
RT "Beta-galactosidase gene fusions as probes for the cytoplasmic regions of
RT subunits I and II of the membrane-bound cytochrome d terminal oxidase from
RT Escherichia coli.";
RL J. Biol. Chem. 263:13130-13137(1988).
RN [10]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF HIS-19; HIS-86; HIS-126; HIS-186;
RP HIS-314 AND HIS-510.
RX PubMed=2656671; DOI=10.1016/s0021-9258(18)83145-3;
RA Fang H., Lin R.J., Gennis R.B.;
RT "Location of heme axial ligands in the cytochrome d terminal oxidase
RT complex of Escherichia coli determined by site-directed mutagenesis.";
RL J. Biol. Chem. 264:8026-8032(1989).
RN [11]
RP DOMAINS.
RX PubMed=1689724; DOI=10.1016/s0021-9258(19)39558-4;
RA Dueweke T.J., Gennis R.B.;
RT "Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity
RT of Escherichia coli cytochrome d complex localize functional domain.";
RL J. Biol. Chem. 265:4273-4277(1990).
RN [12]
RP CATALYTIC ACTIVITY.
RX PubMed=1850294; DOI=10.1021/bi00230a019;
RA Puustinen A., Finel M., Haltia T., Gennis R.B., Wikstroem M.;
RT "Properties of the two terminal oxidases of Escherichia coli.";
RL Biochemistry 30:3936-3942(1991).
RN [13]
RP TOPOLOGY.
RX PubMed=1724280; DOI=10.1111/j.1365-2958.1991.tb02097.x;
RA Newton G., Yun C.H., Gennis R.B.;
RT "Analysis of the topology of the cytochrome d terminal oxidase complex of
RT Escherichia coli by alkaline phosphatase fusions.";
RL Mol. Microbiol. 5:2511-2518(1991).
RN [14]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF MET-393.
RX PubMed=7577938; DOI=10.1021/bi00041a029;
RA Kaysser T.M., Ghaim J.B., Georgiou C., Gennis R.B.;
RT "Methionine-393 is an axial ligand of the heme b558 component of the
RT cytochrome bd ubiquinol oxidase from Escherichia coli.";
RL Biochemistry 34:13491-13501(1995).
RN [15]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15013751; DOI=10.1016/s0014-5793(04)00125-5;
RA Zhang J., Barquera B., Gennis R.B.;
RT "Gene fusions with beta-lactamase show that subunit I of the cytochrome bd
RT quinol oxidase from E. coli has nine transmembrane helices with the O2
RT reactive site near the periplasmic surface.";
RL FEBS Lett. 561:58-62(2004).
RN [16]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [17]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [18]
RP FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=19542282; DOI=10.1128/jb.00562-09;
RA Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.;
RT "Respiration of Escherichia coli can be fully uncoupled via the
RT nonelectrogenic terminal cytochrome bd-II oxidase.";
RL J. Bacteriol. 191:5510-5517(2009).
RN [19]
RP FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=21987791; DOI=10.1073/pnas.1108217108;
RA Borisov V.B., Murali R., Verkhovskaya M.L., Bloch D.A., Han H.,
RA Gennis R.B., Verkhovsky M.I.;
RT "Aerobic respiratory chain of Escherichia coli is not allowed to work in
RT fully uncoupled mode.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17320-17324(2011).
RN [20]
RP PROBABLE INTERACTION WITH CYDX, POSSIBLE INTERACTION WITH APPX, SUBUNIT,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23749980; DOI=10.1128/jb.00324-13;
RA Vanorsdel C.E., Bhatt S., Allen R.J., Brenner E.P., Hobson J.J., Jamil A.,
RA Haynes B.M., Genson A.M., Hemm M.R.;
RT "The Escherichia coli CydX protein is a member of the CydAB cytochrome bd
RT oxidase complex and is required for cytochrome bd oxidase activity.";
RL J. Bacteriol. 195:3640-3650(2013).
RN [21]
RP FORMYLATION AT MET-1.
RC STRAIN=K12 / CAG12184;
RX PubMed=26017780; DOI=10.1002/pmic.201500027;
RA Bienvenut W.V., Giglione C., Meinnel T.;
RT "Proteome-wide analysis of the amino terminal status of Escherichia coli
RT proteins at the steady-state and upon deformylation inhibition.";
RL Proteomics 15:2503-2518(2015).
RN [22]
RP REVIEW.
RX PubMed=21756872; DOI=10.1016/j.bbabio.2011.06.016;
RA Borisov V.B., Gennis R.B., Hemp J., Verkhovsky M.I.;
RT "The cytochrome bd respiratory oxygen reductases.";
RL Biochim. Biophys. Acta 1807:1398-1413(2011).
CC -!- FUNCTION: A terminal oxidase that produces a proton motive force by the
CC vectorial transfer of protons across the inner membrane. It is the
CC component of the aerobic respiratory chain of E.coli that predominates
CC when cells are grown at low aeration. Generates a proton motive force
CC using protons and electrons from opposite sides of the membrane to
CC generate H(2)O, transferring 1 proton/electron.
CC {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791,
CC ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:6307994,
CC ECO:0000269|PubMed:7577938}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4
CC H(+)(out) + 2 H2O(in); Xref=Rhea:RHEA:40527, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.7;
CC Evidence={ECO:0000269|PubMed:1850294, ECO:0000269|PubMed:6307994};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
CC ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
CC ECO:0000269|PubMed:7577938};
CC Note=Binds 1 protoheme IX center (heme b558) per subunit.
CC {ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
CC ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
CC ECO:0000269|PubMed:7577938};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
CC ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
CC ECO:0000269|PubMed:7577938};
CC Note=Binds 1 protoheme IX center (heme b595, originally called
CC cytochrome a1) per heterodimer, in conjunction with CydB.
CC {ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
CC ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
CC ECO:0000269|PubMed:7577938};
CC -!- COFACTOR:
CC Name=heme d cis-diol; Xref=ChEBI:CHEBI:62814;
CC Evidence={ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:3013298,
CC ECO:0000269|PubMed:3013299, ECO:0000269|PubMed:6307994,
CC ECO:0000269|PubMed:7577938};
CC Note=Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in
CC conjunction with CydB. {ECO:0000269|PubMed:2656671,
CC ECO:0000269|PubMed:3013298, ECO:0000269|PubMed:3013299,
CC ECO:0000269|PubMed:6307994, ECO:0000269|PubMed:7577938};
CC -!- ACTIVITY REGULATION: 90% inhibited by cyanide and 2-heptyl-4-
CC hydroxyquinoline N-oxide, at 1 mM and 40 uM respectively.
CC {ECO:0000269|PubMed:6307994}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for ubiquinol-1 {ECO:0000269|PubMed:6307994};
CC KM=0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine
CC {ECO:0000269|PubMed:6307994};
CC KM=0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine
CC {ECO:0000269|PubMed:6307994};
CC Vmax=383 umol/min/mg enzyme for ubiquinol-1
CC {ECO:0000269|PubMed:6307994};
CC Vmax=270 umol/min/mg enzyme for 2,3,5,6-tetramethyl-p-
CC phenylenediamine {ECO:0000269|PubMed:6307994};
CC Vmax=126 umol/min/mg enzyme for N,N,N',N'-tetramethyl-p-
CC phenylenediamine {ECO:0000269|PubMed:6307994};
CC Note=pH 7.0, 37 degrees Celsius.;
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Heterodimer of subunits I and II. Probably interacts with
CC CydX, and overexpressed AppX. {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:23749980, ECO:0000269|PubMed:3281937,
CC ECO:0000269|PubMed:6307994}.
CC -!- INTERACTION:
CC P0ABJ9; P0ABK2: cydB; NbExp=5; IntAct=EBI-906928, EBI-1213195;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15013751,
CC ECO:0000269|PubMed:16079137}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15013751, ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: Under conditions of low aeration, in stationary phase (at
CC protein level). {ECO:0000269|PubMed:6307994}.
CC -!- PTM: 86% of isolated protein was N-formylated.
CC {ECO:0000269|PubMed:26017780, ECO:0000269|PubMed:3281937}.
CC -!- DISRUPTION PHENOTYPE: A double cydA/cydB deletion shows increased
CC sensitivity to reductant (beta-mercapoethanol).
CC {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791,
CC ECO:0000269|PubMed:23749980}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000305}.
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DR EMBL; J03939; AAA18804.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC73827.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35399.1; -; Genomic_DNA.
DR RefSeq; NP_415261.2; NC_000913.3.
DR RefSeq; WP_000884361.1; NZ_SSZK01000033.1.
DR PDB; 6RKO; EM; 2.68 A; A=1-522.
DR PDB; 6RX4; EM; 3.30 A; A=1-522.
DR PDBsum; 6RKO; -.
DR PDBsum; 6RX4; -.
DR AlphaFoldDB; P0ABJ9; -.
DR EMDB; EMD-10049; -.
DR EMDB; EMD-4908; -.
DR SMR; P0ABJ9; -.
DR BioGRID; 4263539; 372.
DR ComplexPortal; CPX-268; Cytochrome bd-I ubiquinol oxidase complex.
DR DIP; DIP-36181N; -.
DR IntAct; P0ABJ9; 4.
DR MINT; P0ABJ9; -.
DR STRING; 511145.b0733; -.
DR TCDB; 3.D.4.3.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR jPOST; P0ABJ9; -.
DR PaxDb; 511145-b0733; -.
DR EnsemblBacteria; AAC73827; AAC73827; b0733.
DR GeneID; 75205564; -.
DR GeneID; 945341; -.
DR KEGG; ecj:JW0722; -.
DR KEGG; eco:b0733; -.
DR PATRIC; fig|1411691.4.peg.1540; -.
DR EchoBASE; EB0170; -.
DR eggNOG; COG1271; Bacteria.
DR HOGENOM; CLU_030555_3_3_6; -.
DR InParanoid; P0ABJ9; -.
DR OMA; TLARWQF; -.
DR OrthoDB; 9807042at2; -.
DR PhylomeDB; P0ABJ9; -.
DR BioCyc; EcoCyc:CYDA-MONOMER; -.
DR BioCyc; MetaCyc:CYDA-MONOMER; -.
DR BRENDA; 7.1.1.7; 2026.
DR UniPathway; UPA00705; -.
DR PRO; PR:P0ABJ9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IDA:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IDA:EcoCyc.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IBA:GO_Central.
DR GO; GO:0019646; P:aerobic electron transport chain; IDA:EcoCyc.
DR GO; GO:0006119; P:oxidative phosphorylation; NAS:ComplexPortal.
DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365:SF0; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR30365; CYTOCHROME D UBIQUINOL OXIDASE; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 1.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; Formylation; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..522
FT /note="Cytochrome bd-I ubiquinol oxidase subunit 1"
FT /id="PRO_0000183919"
FT TOPO_DOM 1..15
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..35
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 36..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..69
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 70..96
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..114
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 115..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..146
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 147..186
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..203
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 204..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 220..235
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 236..390
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 391..407
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 408..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 424..441
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 442..472
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..487
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 488..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 19
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b595"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 186
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b558"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 393
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b558"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:26017780,
FT ECO:0000269|PubMed:3281937"
FT MUTAGEN 19
FT /note="H->L,R: Loss of cytochrome b595 and heme d, no
FT aerobic growth, complex assembles."
FT /evidence="ECO:0000269|PubMed:2656671"
FT MUTAGEN 86
FT /note="H->R: No effect."
FT /evidence="ECO:0000269|PubMed:2656671"
FT MUTAGEN 126
FT /note="H->P: Loss of all cofactors, no aerobic growth,
FT complex assembles."
FT /evidence="ECO:0000269|PubMed:2656671"
FT MUTAGEN 126
FT /note="H->R: No effect."
FT /evidence="ECO:0000269|PubMed:2656671"
FT MUTAGEN 186
FT /note="H->L: Loss of cytochrome b558, no aerobic growth,
FT complex assembles, this subunit is more susceptible to
FT proteolysis."
FT /evidence="ECO:0000269|PubMed:2656671"
FT MUTAGEN 314
FT /note="H->L: Grows aerobically, has altered cytochrome b/d
FT ratio, complex assembles."
FT /evidence="ECO:0000269|PubMed:2656671"
FT MUTAGEN 314
FT /note="H->P: Loss of cytochrome b595 and heme d, no aerobic
FT growth, loss of complex."
FT /evidence="ECO:0000269|PubMed:2656671"
FT MUTAGEN 393
FT /note="M->L: Cytochrome b558 shifts to a high spin
FT configuration, complex assembles. Retains about 1% quinol
FT oxidoreductase activity after purification."
FT MUTAGEN 510
FT /note="H->L: No effect."
FT /evidence="ECO:0000269|PubMed:2656671"
FT CONFLICT 213
FT /note="F -> L (in Ref. 1; AAA18804)"
FT /evidence="ECO:0000305"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:6RKO"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 23..43
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 47..79
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 82..102
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:6RKO"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 123..152
FT /evidence="ECO:0007829|PDB:6RKO"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6RKO"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:6RKO"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 178..209
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 213..236
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 312..332
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6RKO"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:6RKO"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6RX4"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 383..412
FT /evidence="ECO:0007829|PDB:6RKO"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6RX4"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 431..445
FT /evidence="ECO:0007829|PDB:6RKO"
FT TURN 446..450
FT /evidence="ECO:0007829|PDB:6RKO"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:6RKO"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 468..499
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 500..504
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:6RKO"
SQ SEQUENCE 522 AA; 58205 MW; E757442068BCFCFE CRC64;
MLDIVELSRL QFALTAMYHF LFVPLTLGMA FLLAIMETVY VLSGKQIYKD MTKFWGKLFG
INFALGVATG LTMEFQFGTN WSYYSHYVGD IFGAPLAIEG LMAFFLESTF VGLFFFGWDR
LGKVQHMCVT WLVALGSNLS ALWILVANGW MQNPIASDFN FETMRMEMVS FSELVLNPVA
QVKFVHTVAS GYVTGAMFIL GISAWYMLKG RDFAFAKRSF AIAASFGMAA VLSVIVLGDE
SGYEMGDVQK TKLAAIEAEW ETQPAPAAFT LFGIPDQEEE TNKFAIQIPY ALGIIATRSV
DTPVIGLKEL MVQHEERIRN GMKAYSLLEQ LRSGSTDQAV RDQFNSMKKD LGYGLLLKRY
TPNVADATEA QIQQATKDSI PRVAPLYFAF RIMVACGFLL LAIIALSFWS VIRNRIGEKK
WLLRAALYGI PLPWIAVEAG WFVAEYGRQP WAIGEVLPTA VANSSLTAGD LIFSMVLICG
LYTLFLVAEL FLMFKFARLG PSSLKTGRYH FEQSSTTTQP AR
//
