YHJA_ECOLI
ID YHJA_ECOLI Reviewed; 465 AA.
AC P37197; Q2M7I0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Probable cytochrome c peroxidase;
DE EC=1.11.1.5;
GN Name=yhjA; OrderedLocusNames=b3518, JW3486;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
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 [3]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC -!- PTM: Binds 3 heme c groups covalently per subunit. {ECO:0000305}.
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DR EMBL; U00039; AAB18494.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76543.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77776.1; -; Genomic_DNA.
DR PIR; S47738; S47738.
DR RefSeq; NP_417975.1; NC_000913.3.
DR RefSeq; WP_000784827.1; NZ_SSZK01000039.1.
DR AlphaFoldDB; P37197; -.
DR SMR; P37197; -.
DR BioGRID; 4262525; 14.
DR IntAct; P37197; 2.
DR STRING; 511145.b3518; -.
DR jPOST; P37197; -.
DR PaxDb; P37197; -.
DR PRIDE; P37197; -.
DR EnsemblBacteria; AAC76543; AAC76543; b3518.
DR EnsemblBacteria; BAE77776; BAE77776; BAE77776.
DR GeneID; 948038; -.
DR KEGG; ecj:JW3486; -.
DR KEGG; eco:b3518; -.
DR PATRIC; fig|1411691.4.peg.3200; -.
DR EchoBASE; EB2155; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_2_0_6; -.
DR InParanoid; P37197; -.
DR OMA; KGPINAP; -.
DR PhylomeDB; P37197; -.
DR BioCyc; EcoCyc:EG12244-MON; -.
DR BioCyc; MetaCyc:EG12244-MON; -.
DR PRO; PR:P37197; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:EcoCyc.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IMP:EcoCyc.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:EcoCyc.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR025992; Haem-bd.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF14376; Haem_bd; 1.
DR SMART; SM01235; Haem_bd; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 3.
PE 4: Predicted;
KW Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome; Transport.
FT CHAIN 1..465
FT /note="Probable cytochrome c peroxidase"
FT /id="PRO_0000108444"
FT BINDING 59
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 62
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 63
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 195
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 207
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 210
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 211
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 351
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 354
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 355
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 415
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 429
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:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 465 AA; 51571 MW; 9F494A698949E6DA CRC64;
MKMVSRITAI GLAGVAICYL GLSGYVWYHD NKRSKQADVQ ASAVSENNKV LGFLREKGCD
YCHTPSAELP AYYYIPGAKQ LMDYDIKLGY KSFNLEAVRA ALLADKPVSQ SDLNKIEWVM
QYETMPPTRY TALHWAGKVS DEERAEILAW IAKQRAEYYA SNDTAPEHRN EPVQPIPQKL
PTDAQKVALG FALYHDPRLS ADSTISCAHC HALNAGGVDG RKTSIGVGGA VGPINAPTVF
NSVFNVEQFW DGRAATLQDQ AGGPPLNPIE MASKSWDEII AKLEKDPQLK TQFLEVYPQG
FSGENITDAI AEFEKTLITP DSPFDKWLRG DENALTAQQK KGYQLFKDNK CATCHGGIIL
GGRSFEPLGL KKDFNFGEIT AADIGRMNVT KEERDKLRQK VPGLRNVALT APYFHRGDVP
TLDGAVKLML RYQVGKELPQ EDVDDIVAFL HSLNGVYTPY MQDKQ
